CINXE.COM

<!DOCTYPE html> <html class="client-nojs vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-sticky-header-enabled vector-toc-available" lang="en" dir="ltr"> <head> <meta charset="UTF-8"> <title>Enzyme inhibitor - Wikipedia</title> <script>(function(){var className="client-js vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-sticky-header-enabled vector-toc-available";var cookie=document.cookie.match(/(?:^|; )enwikimwclientpreferences=([^;]+)/);if(cookie){cookie[1].split('%2C').forEach(function(pref){className=className.replace(new RegExp('(^| )'+pref.replace(/-clientpref-\w+$|[^\w-]+/g,'')+'-clientpref-\\w+( |$)'),'$1'+pref+'$2');});}document.documentElement.className=className;}());RLCONF={"wgBreakFrames":false,"wgSeparatorTransformTable":["",""],"wgDigitTransformTable":["",""],"wgDefaultDateFormat":"dmy","wgMonthNames":["","January","February","March","April","May","June","July","August","September","October","November","December"],"wgRequestId":"e63af2c9-2c7c-4514-97fa-5202e27bea34","wgCanonicalNamespace":"","wgCanonicalSpecialPageName":false,"wgNamespaceNumber":0,"wgPageName":"Enzyme_inhibitor","wgTitle":"Enzyme inhibitor","wgCurRevisionId":1246407205,"wgRevisionId":1246407205,"wgArticleId":5464960,"wgIsArticle":true,"wgIsRedirect":false,"wgAction":"view","wgUserName":null,"wgUserGroups":["*"],"wgCategories":["Articles with short description","Short description is different from Wikidata","Wikipedia indefinitely move-protected pages","Featured articles","Use dmy dates from July 2022","Articles containing potentially dated statements from 2017","All articles containing potentially dated statements","Pages that use a deprecated format of the chem tags","Biochemical reactions","Medicinal chemistry","Metabolism","Enzyme inhibitors"],"wgPageViewLanguage":"en","wgPageContentLanguage":"en","wgPageContentModel":"wikitext","wgRelevantPageName":"Enzyme_inhibitor","wgRelevantArticleId":5464960,"wgIsProbablyEditable":true,"wgRelevantPageIsProbablyEditable":true,"wgRestrictionEdit":[],"wgRestrictionMove":["sysop"],"wgNoticeProject":"wikipedia","wgCiteReferencePreviewsActive":false,"wgFlaggedRevsParams":{"tags":{"status":{"levels":1}}},"wgMediaViewerOnClick":true,"wgMediaViewerEnabledByDefault":true,"wgPopupsFlags":0,"wgVisualEditor":{"pageLanguageCode":"en","pageLanguageDir":"ltr","pageVariantFallbacks":"en"},"wgMFDisplayWikibaseDescriptions":{"search":true,"watchlist":true,"tagline":false,"nearby":true},"wgWMESchemaEditAttemptStepOversample":false,"wgWMEPageLength":100000,"wgEditSubmitButtonLabelPublish":true,"wgULSPosition":"interlanguage","wgULSisCompactLinksEnabled":false,"wgVector2022LanguageInHeader":true,"wgULSisLanguageSelectorEmpty":false,"wgWikibaseItemId":"Q427492","wgCheckUserClientHintsHeadersJsApi":["brands","architecture","bitness","fullVersionList","mobile","model","platform","platformVersion"],"GEHomepageSuggestedEditsEnableTopics":true,"wgGETopicsMatchModeEnabled":false,"wgGELevelingUpEnabledForUser":false}; RLSTATE={"ext.globalCssJs.user.styles":"ready","site.styles":"ready","user.styles":"ready","ext.globalCssJs.user":"ready","user":"ready","user.options":"loading","ext.cite.styles":"ready","ext.math.styles":"ready","skins.vector.search.codex.styles":"ready","skins.vector.styles":"ready","skins.vector.icons":"ready","jquery.makeCollapsible.styles":"ready","ext.wikimediamessages.styles":"ready","ext.visualEditor.desktopArticleTarget.noscript":"ready","ext.uls.interlanguage":"ready","wikibase.client.init":"ready","ext.wikimediaBadges":"ready"};RLPAGEMODULES=["ext.cite.ux-enhancements","mediawiki.page.media","site","mediawiki.page.ready","jquery.makeCollapsible","mediawiki.toc","skins.vector.js","ext.centralNotice.geoIP","ext.centralNotice.startUp","ext.gadget.ReferenceTooltips","ext.gadget.switcher","ext.urlShortener.toolbar","ext.centralauth.centralautologin","mmv.bootstrap","ext.popups","ext.visualEditor.desktopArticleTarget.init","ext.visualEditor.targetLoader","ext.echo.centralauth","ext.eventLogging","ext.wikimediaEvents","ext.navigationTiming","ext.uls.interface","ext.cx.eventlogging.campaigns","ext.cx.uls.quick.actions","wikibase.client.vector-2022","ext.checkUser.clientHints","ext.quicksurveys.init","ext.growthExperiments.SuggestedEditSession"];</script> <script>(RLQ=window.RLQ||[]).push(function(){mw.loader.impl(function(){return["user.options@12s5i",function($,jQuery,require,module){mw.user.tokens.set({"patrolToken":"+\\","watchToken":"+\\","csrfToken":"+\\"}); }];});});</script> <link rel="stylesheet" href="/w/load.php?lang=en&modules=ext.cite.styles%7Cext.math.styles%7Cext.uls.interlanguage%7Cext.visualEditor.desktopArticleTarget.noscript%7Cext.wikimediaBadges%7Cext.wikimediamessages.styles%7Cjquery.makeCollapsible.styles%7Cskins.vector.icons%2Cstyles%7Cskins.vector.search.codex.styles%7Cwikibase.client.init&only=styles&skin=vector-2022"> <script async="" src="/w/load.php?lang=en&modules=startup&only=scripts&raw=1&skin=vector-2022"></script> <meta name="ResourceLoaderDynamicStyles" content=""> <link rel="stylesheet" href="/w/load.php?lang=en&modules=site.styles&only=styles&skin=vector-2022"> <meta name="generator" content="MediaWiki 1.44.0-wmf.21"> <meta name="referrer" content="origin"> <meta name="referrer" content="origin-when-cross-origin"> <meta name="robots" content="max-image-preview:standard"> <meta name="format-detection" content="telephone=no"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/d/dd/Enzyme_inhibitors_2.svg/1200px-Enzyme_inhibitors_2.svg.png"> <meta property="og:image:width" content="1200"> <meta property="og:image:height" content="773"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/d/dd/Enzyme_inhibitors_2.svg/960px-Enzyme_inhibitors_2.svg.png"> <meta property="og:image:width" content="800"> <meta property="og:image:height" content="515"> <meta property="og:image:width" content="640"> <meta property="og:image:height" content="412"> <meta name="viewport" content="width=1120"> <meta property="og:title" content="Enzyme inhibitor - Wikipedia"> <meta property="og:type" content="website"> <link rel="preconnect" href="//upload.wikimedia.org"> <link rel="alternate" media="only screen and (max-width: 640px)" href="//en.m.wikipedia.org/wiki/Enzyme_inhibitor"> <link rel="alternate" type="application/x-wiki" title="Edit this page" href="/w/index.php?title=Enzyme_inhibitor&action=edit"> <link rel="apple-touch-icon" href="/static/apple-touch/wikipedia.png"> <link rel="icon" href="/static/favicon/wikipedia.ico"> <link rel="search" type="application/opensearchdescription+xml" href="/w/rest.php/v1/search" title="Wikipedia (en)"> <link rel="EditURI" type="application/rsd+xml" href="//en.wikipedia.org/w/api.php?action=rsd"> <link rel="canonical" href="https://en.wikipedia.org/wiki/Enzyme_inhibitor"> <link rel="license" href="https://creativecommons.org/licenses/by-sa/4.0/deed.en"> <link rel="alternate" type="application/atom+xml" title="Wikipedia Atom feed" href="/w/index.php?title=Special:RecentChanges&feed=atom"> <link rel="dns-prefetch" href="//meta.wikimedia.org" /> <link rel="dns-prefetch" href="login.wikimedia.org"> </head> <body class="skin--responsive skin-vector skin-vector-search-vue mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject mw-editable page-Enzyme_inhibitor rootpage-Enzyme_inhibitor skin-vector-2022 action-view"><a class="mw-jump-link" href="#bodyContent">Jump to content</a> <div class="vector-header-container"> <header class="vector-header mw-header"> <div class="vector-header-start"> <nav class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-dropdown" class="vector-dropdown vector-main-menu-dropdown vector-button-flush-left vector-button-flush-right" title="Main menu" > <input type="checkbox" id="vector-main-menu-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-main-menu-dropdown" class="vector-dropdown-checkbox " aria-label="Main menu" > <label id="vector-main-menu-dropdown-label" for="vector-main-menu-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Main menu </label> <div class="vector-dropdown-content"> <div id="vector-main-menu-unpinned-container" class="vector-unpinned-container"> <div id="vector-main-menu" class="vector-main-menu vector-pinnable-element"> <div class="vector-pinnable-header vector-main-menu-pinnable-header vector-pinnable-header-unpinned" data-feature-name="main-menu-pinned" data-pinnable-element-id="vector-main-menu" data-pinned-container-id="vector-main-menu-pinned-container" data-unpinned-container-id="vector-main-menu-unpinned-container" > <div class="vector-pinnable-header-label">Main menu</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-main-menu.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-main-menu.unpin">hide</button> </div> <div id="p-navigation" class="vector-menu mw-portlet mw-portlet-navigation" > <div class="vector-menu-heading"> Navigation </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-mainpage-description" class="mw-list-item"><a href="/wiki/Main_Page" title="Visit the main page [z]" accesskey="z">Main page</a></li><li id="n-contents" class="mw-list-item"><a href="/wiki/Wikipedia:Contents" title="Guides to browsing Wikipedia">Contents</a></li><li id="n-currentevents" class="mw-list-item"><a href="/wiki/Portal:Current_events" title="Articles related to current events">Current events</a></li><li id="n-randompage" class="mw-list-item"><a href="/wiki/Special:Random" title="Visit a randomly selected article [x]" accesskey="x">Random article</a></li><li id="n-aboutsite" class="mw-list-item"><a href="/wiki/Wikipedia:About" title="Learn about Wikipedia and how it works">About Wikipedia</a></li><li id="n-contactpage" class="mw-list-item"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us" title="How to contact Wikipedia">Contact us</a></li> </ul> </div> </div> <div id="p-interaction" class="vector-menu mw-portlet mw-portlet-interaction" > <div class="vector-menu-heading"> Contribute </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-help" class="mw-list-item"><a href="/wiki/Help:Contents" title="Guidance on how to use and edit Wikipedia">Help</a></li><li id="n-introduction" class="mw-list-item"><a href="/wiki/Help:Introduction" title="Learn how to edit Wikipedia">Learn to edit</a></li><li id="n-portal" class="mw-list-item"><a href="/wiki/Wikipedia:Community_portal" title="The hub for editors">Community portal</a></li><li id="n-recentchanges" class="mw-list-item"><a href="/wiki/Special:RecentChanges" title="A list of recent changes to Wikipedia [r]" accesskey="r">Recent changes</a></li><li id="n-upload" class="mw-list-item"><a href="/wiki/Wikipedia:File_upload_wizard" title="Add images or other media for use on Wikipedia">Upload file</a></li><li id="n-specialpages" class="mw-list-item"><a href="/wiki/Special:SpecialPages">Special pages</a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> <a href="/wiki/Main_Page" class="mw-logo"> <img class="mw-logo-icon" src="/static/images/icons/wikipedia.png" alt="" aria-hidden="true" height="50" width="50"> <img class="mw-logo-wordmark" alt="Wikipedia" src="/static/images/mobile/copyright/wikipedia-wordmark-en.svg" style="width: 7.5em; height: 1.125em;"> <img class="mw-logo-tagline" alt="The Free Encyclopedia" src="/static/images/mobile/copyright/wikipedia-tagline-en.svg" width="117" height="13" style="width: 7.3125em; height: 0.8125em;"> </a> </div> <div class="vector-header-end"> <div id="p-search" role="search" class="vector-search-box-vue vector-search-box-collapses vector-search-box-show-thumbnail vector-search-box-auto-expand-width vector-search-box"> <a href="/wiki/Special:Search" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only search-toggle" title="Search Wikipedia [f]" accesskey="f"> Search </a> <div class="vector-typeahead-search-container"> <div class="cdx-typeahead-search cdx-typeahead-search--show-thumbnail cdx-typeahead-search--auto-expand-width"> <form action="/w/index.php" id="searchform" class="cdx-search-input cdx-search-input--has-end-button"> <div id="simpleSearch" class="cdx-search-input__input-wrapper" data-search-loc="header-moved"> <div class="cdx-text-input cdx-text-input--has-start-icon"> <input class="cdx-text-input__input" type="search" name="search" placeholder="Search Wikipedia" aria-label="Search Wikipedia" autocapitalize="sentences" title="Search Wikipedia [f]" accesskey="f" id="searchInput" > </div> <input type="hidden" name="title" value="Special:Search"> </div> <button class="cdx-button cdx-search-input__end-button">Search</button> </form> </div> </div> </div> <nav class="vector-user-links vector-user-links-wide" aria-label="Personal tools"> <div class="vector-user-links-main"> <div id="p-vector-user-menu-preferences" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-userpage" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-dropdown" class="vector-dropdown " title="Change the appearance of the page's font size, width, and color" > <input type="checkbox" id="vector-appearance-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-appearance-dropdown" class="vector-dropdown-checkbox " aria-label="Appearance" > <label id="vector-appearance-dropdown-label" for="vector-appearance-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Appearance </label> <div class="vector-dropdown-content"> <div id="vector-appearance-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <div id="p-vector-user-menu-notifications" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-overflow" class="vector-menu mw-portlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="https://donate.wikimedia.org/?wmf_source=donate&wmf_medium=sidebar&wmf_campaign=en.wikipedia.org&uselang=en" class="">Donate</a> </li> <li id="pt-createaccount-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:CreateAccount&returnto=Enzyme+inhibitor" title="You are encouraged to create an account and log in; however, it is not mandatory" class="">Create account</a> </li> <li id="pt-login-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:UserLogin&returnto=Enzyme+inhibitor" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o" class="">Log in</a> </li> </ul> </div> </div> </div> <div id="vector-user-links-dropdown" class="vector-dropdown vector-user-menu vector-button-flush-right vector-user-menu-logged-out" title="Log in and more options" > <input type="checkbox" id="vector-user-links-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-user-links-dropdown" class="vector-dropdown-checkbox " aria-label="Personal tools" > <label id="vector-user-links-dropdown-label" for="vector-user-links-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Personal tools </label> <div class="vector-dropdown-content"> <div id="p-personal" class="vector-menu mw-portlet mw-portlet-personal user-links-collapsible-item" title="User menu" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport" class="user-links-collapsible-item mw-list-item"><a href="https://donate.wikimedia.org/?wmf_source=donate&wmf_medium=sidebar&wmf_campaign=en.wikipedia.org&uselang=en">Donate</a></li><li id="pt-createaccount" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:CreateAccount&returnto=Enzyme+inhibitor" title="You are encouraged to create an account and log in; however, it is not mandatory"> Create account</a></li><li id="pt-login" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:UserLogin&returnto=Enzyme+inhibitor" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o"> Log in</a></li> </ul> </div> </div> <div id="p-user-menu-anon-editor" class="vector-menu mw-portlet mw-portlet-user-menu-anon-editor" > <div class="vector-menu-heading"> Pages for logged out editors <a href="/wiki/Help:Introduction" aria-label="Learn more about editing">learn more</a> </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-anoncontribs" class="mw-list-item"><a href="/wiki/Special:MyContributions" title="A list of edits made from this IP address [y]" accesskey="y">Contributions</a></li><li id="pt-anontalk" class="mw-list-item"><a href="/wiki/Special:MyTalk" title="Discussion about edits from this IP address [n]" accesskey="n">Talk</a></li> </ul> </div> </div> </div> </div> </nav> </div> </header> </div> <div class="mw-page-container"> <div class="mw-page-container-inner"> <div class="vector-sitenotice-container"> <div id="siteNotice"></div> </div> <div class="vector-column-start"> <div class="vector-main-menu-container"> <div id="mw-navigation"> <nav id="mw-panel" class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-pinned-container" class="vector-pinned-container"> </div> </nav> </div> </div> <div class="vector-sticky-pinned-container"> <nav id="mw-panel-toc" aria-label="Contents" data-event-name="ui.sidebar-toc" class="mw-table-of-contents-container vector-toc-landmark"> <div id="vector-toc-pinned-container" class="vector-pinned-container"> <div id="vector-toc" class="vector-toc vector-pinnable-element"> <div class="vector-pinnable-header vector-toc-pinnable-header vector-pinnable-header-pinned" data-feature-name="toc-pinned" data-pinnable-element-id="vector-toc" > <h2 class="vector-pinnable-header-label">Contents</h2> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-toc.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-toc.unpin">hide</button> </div> <ul class="vector-toc-contents" id="mw-panel-toc-list"> <li id="toc-mw-content-text" class="vector-toc-list-item vector-toc-level-1"> <a href="#" class="vector-toc-link"> <div class="vector-toc-text">(Top)</div> </a> </li> <li id="toc-Structural_classes" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Structural_classes"> <div class="vector-toc-text"> 1 Structural classes </div> </a> <ul id="toc-Structural_classes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Reversible_inhibitors" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Reversible_inhibitors"> <div class="vector-toc-text"> 2 Reversible inhibitors </div> </a> <button aria-controls="toc-Reversible_inhibitors-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> Toggle Reversible inhibitors subsection </button> <ul id="toc-Reversible_inhibitors-sublist" class="vector-toc-list"> <li id="toc-Competitive" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Competitive"> <div class="vector-toc-text"> 2.1 Competitive </div> </a> <ul id="toc-Competitive-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Uncompetitive" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Uncompetitive"> <div class="vector-toc-text"> 2.2 Uncompetitive </div> </a> <ul id="toc-Uncompetitive-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Non-competitive" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Non-competitive"> <div class="vector-toc-text"> 2.3 Non-competitive </div> </a> <ul id="toc-Non-competitive-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Mixed" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Mixed"> <div class="vector-toc-text"> 2.4 Mixed </div> </a> <ul id="toc-Mixed-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Quantitative_description" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Quantitative_description"> <div class="vector-toc-text"> 2.5 Quantitative description </div> </a> <ul id="toc-Quantitative_description-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Dissociation_constants" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Dissociation_constants"> <div class="vector-toc-text"> 2.6 Dissociation constants </div> </a> <ul id="toc-Dissociation_constants-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Special_cases" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Special_cases"> <div class="vector-toc-text"> 2.7 Special cases </div> </a> <ul id="toc-Special_cases-sublist" class="vector-toc-list"> <li id="toc-Partially_competitive" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Partially_competitive"> <div class="vector-toc-text"> 2.7.1 Partially competitive </div> </a> <ul id="toc-Partially_competitive-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Substrate_or_product" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Substrate_or_product"> <div class="vector-toc-text"> 2.7.2 Substrate or product </div> </a> <ul id="toc-Substrate_or_product-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Slow-tight" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Slow-tight"> <div class="vector-toc-text"> 2.7.3 Slow-tight </div> </a> <ul id="toc-Slow-tight-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Multi-substrate_analogues" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Multi-substrate_analogues"> <div class="vector-toc-text"> 2.7.4 Multi-substrate analogues </div> </a> <ul id="toc-Multi-substrate_analogues-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Examples" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Examples"> <div class="vector-toc-text"> 2.8 Examples </div> </a> <ul id="toc-Examples-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Irreversible_inhibitors" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Irreversible_inhibitors"> <div class="vector-toc-text"> 3 Irreversible inhibitors </div> </a> <button aria-controls="toc-Irreversible_inhibitors-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> Toggle Irreversible inhibitors subsection </button> <ul id="toc-Irreversible_inhibitors-sublist" class="vector-toc-list"> <li id="toc-Types" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Types"> <div class="vector-toc-text"> 3.1 Types </div> </a> <ul id="toc-Types-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Measuring" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Measuring"> <div class="vector-toc-text"> 3.2 Measuring </div> </a> <ul id="toc-Measuring-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Slow_binding" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Slow_binding"> <div class="vector-toc-text"> 3.3 Slow binding </div> </a> <ul id="toc-Slow_binding-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Some_examples" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Some_examples"> <div class="vector-toc-text"> 3.4 Some examples </div> </a> <ul id="toc-Some_examples-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Applications" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Applications"> <div class="vector-toc-text"> 4 Applications </div> </a> <button aria-controls="toc-Applications-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> Toggle Applications subsection </button> <ul id="toc-Applications-sublist" class="vector-toc-list"> <li id="toc-Metabolic_regulation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Metabolic_regulation"> <div class="vector-toc-text"> 4.1 Metabolic regulation </div> </a> <ul id="toc-Metabolic_regulation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Natural_poisons" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Natural_poisons"> <div class="vector-toc-text"> 4.2 Natural poisons </div> </a> <ul id="toc-Natural_poisons-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Drugs" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Drugs"> <div class="vector-toc-text"> 4.3 Drugs </div> </a> <ul id="toc-Drugs-sublist" class="vector-toc-list"> <li id="toc-Antibiotics" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Antibiotics"> <div class="vector-toc-text"> 4.3.1 Antibiotics </div> </a> <ul id="toc-Antibiotics-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Antivirals" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Antivirals"> <div class="vector-toc-text"> 4.3.2 Antivirals </div> </a> <ul id="toc-Antivirals-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Pesticides" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Pesticides"> <div class="vector-toc-text"> 4.4 Pesticides </div> </a> <ul id="toc-Pesticides-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Herbicides" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Herbicides"> <div class="vector-toc-text"> 4.5 Herbicides </div> </a> <ul id="toc-Herbicides-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Discovery_and_design" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Discovery_and_design"> <div class="vector-toc-text"> 5 Discovery and design </div> </a> <ul id="toc-Discovery_and_design-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> 6 See also </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> 7 References </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> 8 External links </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" title="Table of Contents" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Toggle the table of contents </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading">Enzyme inhibitor</h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 33 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-33" aria-hidden="true" > 33 languages </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D9%85%D8%AB%D8%A8%D8%B7_%D8%A5%D9%86%D8%B2%D9%8A%D9%85" title="مثبط إنزيم – Arabic" lang="ar" hreflang="ar" data-title="مثبط إنزيم" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target">العربية</a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Inhibitor_enzima" title="Inhibitor enzima – Bosnian" lang="bs" hreflang="bs" data-title="Inhibitor enzima" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target">Bosanski</a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Inhibidor_enzim%C3%A0tic" title="Inhibidor enzimàtic – Catalan" lang="ca" hreflang="ca" data-title="Inhibidor enzimàtic" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target">Català</a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Inhibice" title="Inhibice – Czech" lang="cs" hreflang="cs" data-title="Inhibice" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target">Čeština</a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Enzyminhibitor" title="Enzyminhibitor – Danish" lang="da" hreflang="da" data-title="Enzyminhibitor" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target">Dansk</a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Enzymhemmung" title="Enzymhemmung – German" lang="de" hreflang="de" data-title="Enzymhemmung" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target">Deutsch</a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Ens%C3%BC%C3%BCmiinhibiitor" title="Ensüümiinhibiitor – Estonian" lang="et" hreflang="et" data-title="Ensüümiinhibiitor" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target">Eesti</a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%91%CE%BD%CE%B1%CF%83%CF%84%CE%BF%CE%BB%CE%AD%CE%B1%CF%82_%CE%B5%CE%BD%CE%B6%CF%8D%CE%BC%CE%BF%CF%85" title="Αναστολέας ενζύμου – Greek" lang="el" hreflang="el" data-title="Αναστολέας ενζύμου" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target">Ελληνικά</a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Inhibidor_enzim%C3%A1tico" title="Inhibidor enzimático – Spanish" lang="es" hreflang="es" data-title="Inhibidor enzimático" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target">Español</a></li><li class="interlanguage-link interwiki-eu mw-list-item"><a href="https://eu.wikipedia.org/wiki/Entzima-inhibitzaile" title="Entzima-inhibitzaile – Basque" lang="eu" hreflang="eu" data-title="Entzima-inhibitzaile" data-language-autonym="Euskara" data-language-local-name="Basque" class="interlanguage-link-target">Euskara</a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%A8%D8%A7%D8%B2%D8%AF%D8%A7%D8%B1%D9%86%D8%AF%D9%87_%D8%A2%D9%86%D8%B2%DB%8C%D9%85" title="بازدارنده آنزیم – Persian" lang="fa" hreflang="fa" data-title="بازدارنده آنزیم" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target">فارسی</a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Inhibiteur_enzymatique" title="Inhibiteur enzymatique – French" lang="fr" hreflang="fr" data-title="Inhibiteur enzymatique" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target">Français</a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Inhibidor_encim%C3%A1tico" title="Inhibidor encimático – Galician" lang="gl" hreflang="gl" data-title="Inhibidor encimático" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target">Galego</a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%ED%9A%A8%EC%86%8C_%EC%A0%80%ED%95%B4%EC%A0%9C" title="효소 저해제 – Korean" lang="ko" hreflang="ko" data-title="효소 저해제" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target">한국어</a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Penghambat_enzim" title="Penghambat enzim – Indonesian" lang="id" hreflang="id" data-title="Penghambat enzim" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target">Bahasa Indonesia</a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Inibitore_enzimatico" title="Inibitore enzimatico – Italian" lang="it" hreflang="it" data-title="Inibitore enzimatico" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target">Italiano</a></li><li class="interlanguage-link interwiki-he badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://he.wikipedia.org/wiki/%D7%9E%D7%A2%D7%9B%D7%91%D7%99_%D7%90%D7%A0%D7%96%D7%99%D7%9E%D7%99%D7%9D" title="מעכבי אנזימים – Hebrew" lang="he" hreflang="he" data-title="מעכבי אנזימים" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target">עברית</a></li><li class="interlanguage-link interwiki-lv mw-list-item"><a href="https://lv.wikipedia.org/wiki/Fermentu_inhibitors" title="Fermentu inhibitors – Latvian" lang="lv" hreflang="lv" data-title="Fermentu inhibitors" data-language-autonym="Latviešu" data-language-local-name="Latvian" class="interlanguage-link-target">Latviešu</a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Perencat_enzim" title="Perencat enzim – Malay" lang="ms" hreflang="ms" data-title="Perencat enzim" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target">Bahasa Melayu</a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Inhibitie_van_enzymen" title="Inhibitie van enzymen – Dutch" lang="nl" hreflang="nl" data-title="Inhibitie van enzymen" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target">Nederlands</a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E9%85%B5%E7%B4%A0%E9%98%BB%E5%AE%B3%E5%89%A4" title="酵素阻害剤 – Japanese" lang="ja" hreflang="ja" data-title="酵素阻害剤" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target">日本語</a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Inibidor_enzim%C3%A1tico" title="Inibidor enzimático – Portuguese" lang="pt" hreflang="pt" data-title="Inibidor enzimático" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target">Português</a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Inhibitor_enzimatic" title="Inhibitor enzimatic – Romanian" lang="ro" hreflang="ro" data-title="Inhibitor enzimatic" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target">Română</a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%98%D0%BD%D0%B3%D0%B8%D0%B1%D0%B8%D1%80%D0%BE%D0%B2%D0%B0%D0%BD%D0%B8%D0%B5_%D1%84%D0%B5%D1%80%D0%BC%D0%B5%D0%BD%D1%82%D0%BE%D0%B2" title="Ингибирование ферментов – Russian" lang="ru" hreflang="ru" data-title="Ингибирование ферментов" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target">Русский</a></li><li class="interlanguage-link interwiki-sq mw-list-item"><a href="https://sq.wikipedia.org/wiki/Frenuesi_i_enzim%C3%ABs" title="Frenuesi i enzimës – Albanian" lang="sq" hreflang="sq" data-title="Frenuesi i enzimës" data-language-autonym="Shqip" data-language-local-name="Albanian" class="interlanguage-link-target">Shqip</a></li><li class="interlanguage-link interwiki-sk mw-list-item"><a href="https://sk.wikipedia.org/wiki/Enz%C3%BDmov%C3%BD_inhib%C3%ADtor" title="Enzýmový inhibítor – Slovak" lang="sk" hreflang="sk" data-title="Enzýmový inhibítor" data-language-autonym="Slovenčina" data-language-local-name="Slovak" class="interlanguage-link-target">Slovenčina</a></li><li class="interlanguage-link interwiki-sl mw-list-item"><a href="https://sl.wikipedia.org/wiki/Encimski_inhibitor" title="Encimski inhibitor – Slovenian" lang="sl" hreflang="sl" data-title="Encimski inhibitor" data-language-autonym="Slovenščina" data-language-local-name="Slovenian" class="interlanguage-link-target">Slovenščina</a></li><li class="interlanguage-link interwiki-sr badge-Q17437796 badge-featuredarticle mw-list-item" title="featured article badge"><a href="https://sr.wikipedia.org/wiki/Inhibitor_enzima" title="Inhibitor enzima – Serbian" lang="sr" hreflang="sr" data-title="Inhibitor enzima" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target">Српски / srpski</a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Inhibitor_enzima" title="Inhibitor enzima – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Inhibitor enzima" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target">Srpskohrvatski / српскохрватски</a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Enzim_inhibit%C3%B6r%C3%BC" title="Enzim inhibitörü – Turkish" lang="tr" hreflang="tr" data-title="Enzim inhibitörü" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target">Türkçe</a></li><li class="interlanguage-link interwiki-tk mw-list-item"><a href="https://tk.wikipedia.org/wiki/Fermentatiw_ingibitor" title="Fermentatiw ingibitor – Turkmen" lang="tk" hreflang="tk" data-title="Fermentatiw ingibitor" data-language-autonym="Türkmençe" data-language-local-name="Turkmen" class="interlanguage-link-target">Türkmençe</a></li><li class="interlanguage-link interwiki-vi mw-list-item"><a href="https://vi.wikipedia.org/wiki/Ch%E1%BA%A5t_%E1%BB%A9c_ch%E1%BA%BF_enzym" title="Chất ức chế enzym – Vietnamese" lang="vi" hreflang="vi" data-title="Chất ức chế enzym" data-language-autonym="Tiếng Việt" data-language-local-name="Vietnamese" class="interlanguage-link-target">Tiếng Việt</a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E9%85%B6%E6%8A%91%E5%88%B6%E5%89%82" title="酶抑制剂 – Chinese" lang="zh" hreflang="zh" data-title="酶抑制剂" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target">中文</a></li> </ul> <div class="after-portlet after-portlet-lang"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q427492#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div id="left-navigation"> <nav aria-label="Namespaces"> <div id="p-associated-pages" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-associated-pages" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-nstab-main" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Enzyme_inhibitor" title="View the content page [c]" accesskey="c">Article</a></li><li id="ca-talk" class="vector-tab-noicon mw-list-item"><a href="/wiki/Talk:Enzyme_inhibitor" rel="discussion" title="Discuss improvements to the content page [t]" accesskey="t">Talk</a></li> </ul> </div> </div> <div id="vector-variants-dropdown" class="vector-dropdown emptyPortlet" > <input type="checkbox" id="vector-variants-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-variants-dropdown" class="vector-dropdown-checkbox " aria-label="Change language variant" > <label id="vector-variants-dropdown-label" for="vector-variants-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" >English </label> <div class="vector-dropdown-content"> <div id="p-variants" class="vector-menu mw-portlet mw-portlet-variants emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> </div> </div> </nav> </div> <div id="right-navigation" class="vector-collapsible"> <nav aria-label="Views"> <div id="p-views" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-views" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-view" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Enzyme_inhibitor">Read</a></li><li id="ca-edit" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&action=edit" title="Edit this page [e]" accesskey="e">Edit</a></li><li id="ca-history" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&action=history" title="Past revisions of this page [h]" accesskey="h">View history</a></li> </ul> </div> </div> </nav> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-dropdown" class="vector-dropdown vector-page-tools-dropdown" > <input type="checkbox" id="vector-page-tools-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-tools-dropdown" class="vector-dropdown-checkbox " aria-label="Tools" > <label id="vector-page-tools-dropdown-label" for="vector-page-tools-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" >Tools </label> <div class="vector-dropdown-content"> <div id="vector-page-tools-unpinned-container" class="vector-unpinned-container"> <div id="vector-page-tools" class="vector-page-tools vector-pinnable-element"> <div class="vector-pinnable-header vector-page-tools-pinnable-header vector-pinnable-header-unpinned" data-feature-name="page-tools-pinned" data-pinnable-element-id="vector-page-tools" data-pinned-container-id="vector-page-tools-pinned-container" data-unpinned-container-id="vector-page-tools-unpinned-container" > <div class="vector-pinnable-header-label">Tools</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-page-tools.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-page-tools.unpin">hide</button> </div> <div id="p-cactions" class="vector-menu mw-portlet mw-portlet-cactions emptyPortlet vector-has-collapsible-items" title="More options" > <div class="vector-menu-heading"> Actions </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-more-view" class="selected vector-more-collapsible-item mw-list-item"><a href="/wiki/Enzyme_inhibitor">Read</a></li><li id="ca-more-edit" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&action=edit" title="Edit this page [e]" accesskey="e">Edit</a></li><li id="ca-more-history" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&action=history">View history</a></li> </ul> </div> </div> <div id="p-tb" class="vector-menu mw-portlet mw-portlet-tb" > <div class="vector-menu-heading"> General </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="t-whatlinkshere" class="mw-list-item"><a href="/wiki/Special:WhatLinksHere/Enzyme_inhibitor" title="List of all English Wikipedia pages containing links to this page [j]" accesskey="j">What links here</a></li><li id="t-recentchangeslinked" class="mw-list-item"><a href="/wiki/Special:RecentChangesLinked/Enzyme_inhibitor" rel="nofollow" title="Recent changes in pages linked from this page [k]" accesskey="k">Related changes</a></li><li id="t-upload" class="mw-list-item"><a href="//en.wikipedia.org/wiki/Wikipedia:File_Upload_Wizard" title="Upload files [u]" accesskey="u">Upload file</a></li><li id="t-permalink" class="mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&oldid=1246407205" title="Permanent link to this revision of this page">Permanent link</a></li><li id="t-info" class="mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&action=info" title="More information about this page">Page information</a></li><li id="t-cite" class="mw-list-item"><a href="/w/index.php?title=Special:CiteThisPage&page=Enzyme_inhibitor&id=1246407205&wpFormIdentifier=titleform" title="Information on how to cite this page">Cite this page</a></li><li id="t-urlshortener" class="mw-list-item"><a href="/w/index.php?title=Special:UrlShortener&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FEnzyme_inhibitor">Get shortened URL</a></li><li id="t-urlshortener-qrcode" class="mw-list-item"><a href="/w/index.php?title=Special:QrCode&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FEnzyme_inhibitor">Download QR code</a></li> </ul> </div> </div> <div id="p-coll-print_export" class="vector-menu mw-portlet mw-portlet-coll-print_export" > <div class="vector-menu-heading"> Print/export </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="coll-download-as-rl" class="mw-list-item"><a href="/w/index.php?title=Special:DownloadAsPdf&page=Enzyme_inhibitor&action=show-download-screen" title="Download this page as a PDF file">Download as PDF</a></li><li id="t-print" class="mw-list-item"><a href="/w/index.php?title=Enzyme_inhibitor&printable=yes" title="Printable version of this page [p]" accesskey="p">Printable version</a></li> </ul> </div> </div> <div id="p-wikibase-otherprojects" class="vector-menu mw-portlet mw-portlet-wikibase-otherprojects" > <div class="vector-menu-heading"> In other projects </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="wb-otherproject-link wb-otherproject-commons mw-list-item"><a href="https://commons.wikimedia.org/wiki/Category:Enzyme_inhibitors" hreflang="en">Wikimedia Commons</a></li><li id="t-wikibase" class="wb-otherproject-link wb-otherproject-wikibase-dataitem mw-list-item"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q427492" title="Structured data on this page hosted by Wikidata [g]" accesskey="g">Wikidata item</a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> </div> </div> </div> <div class="vector-column-end"> <div class="vector-sticky-pinned-container"> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-pinned-container" class="vector-pinned-container"> </div> </nav> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-pinned-container" class="vector-pinned-container"> <div id="vector-appearance" class="vector-appearance vector-pinnable-element"> <div class="vector-pinnable-header vector-appearance-pinnable-header vector-pinnable-header-pinned" data-feature-name="appearance-pinned" data-pinnable-element-id="vector-appearance" data-pinned-container-id="vector-appearance-pinned-container" data-unpinned-container-id="vector-appearance-unpinned-container" > <div class="vector-pinnable-header-label">Appearance</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-appearance.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-appearance.unpin">hide</button> </div> </div> </div> </nav> </div> </div> <div id="bodyContent" class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> <div id="mw-indicator-featured-star" class="mw-indicator"><div class="mw-parser-output"><a href="/wiki/Wikipedia:Featured_articles*" title="This is a featured article. Click here for more information."><img alt="Featured article" src="//upload.wikimedia.org/wikipedia/en/thumb/e/e7/Cscr-featured.svg/20px-Cscr-featured.svg.png" decoding="async" width="20" height="19" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/e/e7/Cscr-featured.svg/30px-Cscr-featured.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/e/e7/Cscr-featured.svg/40px-Cscr-featured.svg.png 2x" data-file-width="466" data-file-height="443" /></a></div></div> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Molecule that blocks enzyme activity</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Enzyme_inhibitors_2.svg" class="mw-file-description"><img alt="cartoon depiction of an enzyme binding substrate to its active site and releasing product (top), and an inhibitor binding to the active site, thus preventing substrate binding" src="//upload.wikimedia.org/wikipedia/commons/thumb/d/dd/Enzyme_inhibitors_2.svg/250px-Enzyme_inhibitors_2.svg.png" decoding="async" width="220" height="142" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/dd/Enzyme_inhibitors_2.svg/330px-Enzyme_inhibitors_2.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/dd/Enzyme_inhibitors_2.svg/500px-Enzyme_inhibitors_2.svg.png 2x" data-file-width="1771" data-file-height="1141" /></a><figcaption>Top: <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> (E) accelerates conversion of <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrates</a> (S) to <a href="/wiki/Product_(chemistry)" title="Product (chemistry)">products</a> (P). Bottom: by binding to the enzyme, inhibitor (I) blocks binding of substrate. Binding site shown in blue checkerboard, substrate as black rectangle, and inhibitor as green rounded rectangle.</figcaption></figure> An enzyme inhibitor is a <a href="/wiki/Molecule" title="Molecule">molecule</a> that binds to an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> and blocks its <a href="/wiki/Enzyme_activity" class="mw-redirect" title="Enzyme activity">activity</a>. Enzymes are <a href="/wiki/Protein" title="Protein">proteins</a> that speed up <a href="/wiki/Chemical_reaction" title="Chemical reaction">chemical reactions</a> necessary for <a href="/wiki/Life" title="Life">life</a>, in which <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate molecules</a> are converted into <a href="/wiki/Product_(chemistry)" title="Product (chemistry)">products</a>.<a href="#cite_note-Copeland_2013-1">[1]</a> An enzyme <a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">facilitates</a> a specific chemical reaction by binding the substrate to its <a href="/wiki/Active_site" title="Active site">active site</a>, a specialized area on the enzyme that accelerates the <a href="/wiki/Rate-determining_step" title="Rate-determining step">most difficult step of the reaction</a>. An enzyme inhibitor stops ("inhibits") this process, either by binding to the enzyme's active site (thus preventing the substrate itself from binding) or by binding to another site on the enzyme such that the enzyme's <a href="/wiki/Catalysis" title="Catalysis">catalysis</a> of the reaction is blocked. Enzyme inhibitors may bind <a href="/wiki/Reversible_reaction" title="Reversible reaction">reversibly</a> or irreversibly. Irreversible inhibitors form a <a href="/wiki/Covalent_bond" title="Covalent bond">chemical bond</a> with the enzyme such that the enzyme is inhibited until the chemical bond is broken. By contrast, reversible inhibitors bind <a href="/wiki/Non-covalent_interactions" class="mw-redirect" title="Non-covalent interactions">non-covalently</a> and may spontaneously leave the enzyme, allowing the enzyme to resume its function. Reversible inhibitors produce different types of inhibition depending on whether they bind to the enzyme, the enzyme-substrate complex, or both. Enzyme inhibitors play an important role in all cells, since they are generally specific to one enzyme each and serve to control that enzyme's activity. For example, enzymes in a <a href="/wiki/Metabolic_pathway" title="Metabolic pathway">metabolic pathway</a> may be inhibited by molecules produced later in the pathway, thus curtailing the production of molecules that are no longer needed. This type of <a href="/wiki/Negative_feedback" title="Negative feedback">negative feedback</a> is an important way to maintain <a href="/wiki/Homeostasis" title="Homeostasis">balance</a> in a <a href="/wiki/Cell_(biology)" title="Cell (biology)">cell</a>.<a href="#cite_note-Sauro_2017-2">[2]</a> Enzyme inhibitors also control essential enzymes such as <a href="/wiki/Protease" title="Protease">proteases</a> or <a href="/wiki/Nuclease" title="Nuclease">nucleases</a> that, if left unchecked, may damage a cell. Many <a href="/wiki/Poison" title="Poison">poisons</a> produced by animals or plants are enzyme inhibitors that block the activity of crucial enzymes in prey or <a href="/wiki/Predator" class="mw-redirect" title="Predator">predators</a>. Many <a href="/wiki/Medication" title="Medication">drug molecules</a> are enzyme inhibitors that inhibit an aberrant human enzyme or an enzyme critical for the survival of a <a href="/wiki/Pathogen" title="Pathogen">pathogen</a> such as a <a href="/wiki/Virus" title="Virus">virus</a>, <a href="/wiki/Bacterium" class="mw-redirect" title="Bacterium">bacterium</a> or <a href="/wiki/Parasite" class="mw-redirect" title="Parasite">parasite</a>. Examples include <a href="/wiki/Methotrexate" title="Methotrexate">methotrexate</a> (used in <a href="/wiki/Chemotherapy" title="Chemotherapy">chemotherapy</a> and in treating <a href="/wiki/Rheumatic_arthritis" class="mw-redirect" title="Rheumatic arthritis">rheumatic arthritis</a>) and the <a href="/wiki/Protease_inhibitors" class="mw-redirect" title="Protease inhibitors">protease inhibitors</a> used to treat <a href="/wiki/HIV/AIDS" title="HIV/AIDS">HIV/AIDS</a>. Since anti-pathogen inhibitors generally target only one enzyme, such drugs are highly <a href="/wiki/Specificity_(biochemistry)" class="mw-redirect" title="Specificity (biochemistry)">specific</a> and generally produce few side effects in humans, provided that no <a href="/wiki/Sequence_homology" title="Sequence homology">analogous</a> enzyme is found in humans. (This is often the case, since such <a href="/wiki/Pathogen" title="Pathogen">pathogens</a> and <a href="/wiki/Human" title="Human">humans</a> are <a href="/wiki/Genetic_distance" title="Genetic distance">genetically distant</a>.) Medicinal enzyme inhibitors often have low <a href="/wiki/Dissociation_constant" title="Dissociation constant">dissociation constants</a>, meaning that only a minute amount of the inhibitor is required to inhibit the enzyme. A low concentration of the enzyme inhibitor reduces the risk for <a href="/wiki/Hepatotoxicity" title="Hepatotoxicity">liver</a> and <a href="/wiki/Nephrotoxicity" title="Nephrotoxicity">kidney damage</a> and other <a href="/wiki/Adverse_drug_reaction" title="Adverse drug reaction">adverse drug reactions</a> in humans. Hence the discovery and refinement of enzyme inhibitors is an active area of research in <a href="/wiki/Biochemistry" title="Biochemistry">biochemistry</a> and <a href="/wiki/Pharmacology" title="Pharmacology">pharmacology</a>. <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Structural_classes">Structural classes</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=1" title="Edit section: Structural classes">edit</a>]</div> Enzyme inhibitors are a chemically diverse set of substances that range in size from organic <a href="/wiki/Small_molecule" title="Small molecule">small molecules</a> to macromolecular <a href="/wiki/Protein" title="Protein">proteins</a>. Small molecule inhibitors include essential <a href="/wiki/Primary_metabolite" title="Primary metabolite">primary metabolites</a> that inhibit upstream enzymes that produce those metabolites. This provides a negative feedback loop that prevents over production of metabolites and thus maintains cellular <a href="/wiki/Homeostasis" title="Homeostasis">homeostasis</a> (steady internal conditions).<a href="#cite_note-Plaxton_2004-3">[3]</a><a href="#cite_note-Sauro_2017-2">[2]</a> Small molecule enzyme inhibitors also include <a href="/wiki/Secondary_metabolite" title="Secondary metabolite">secondary metabolites</a>, which are not essential to the organism that produces them, but provide the organism with an evolutionary advantage, in that they can be used to repel predators or competing organisms or immobilize prey.<a href="#cite_note-Haefner_2003-4">[4]</a> In addition, many drugs are small molecule enzyme inhibitors that target either disease-modifying enzymes in the patient<a href="#cite_note-Copeland_2013-1">[1]</a>: 5  or enzymes in pathogens which are required for the growth and reproduction of the pathogen.<a href="#cite_note-Gualerzi_2013-5">[5]</a> In addition to small molecules, some proteins act as enzyme inhibitors. The most prominent example are <a href="/wiki/Serpin" title="Serpin">serpins</a> (serine protease inhibitors) which are produced by animals to protect against inappropriate enzyme activation and by plants to prevent predation.<a href="#cite_note-Sanrattana_2019-6">[6]</a> Another class of inhibitor proteins is the <a href="/wiki/Ribonuclease_inhibitor" title="Ribonuclease inhibitor">ribonuclease inhibitors</a>, which bind to <a href="/wiki/Ribonuclease" title="Ribonuclease">ribonucleases</a> in one of the tightest known <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">protein–protein interactions</a>.<a href="#cite_note-7">[7]</a> A special case of protein enzyme inhibitors are <a href="/wiki/Zymogen" title="Zymogen">zymogens</a> that contain an autoinhibitory <a href="/wiki/N-terminal" class="mw-redirect" title="N-terminal">N-terminal</a> peptide that binds to the active site of enzyme that <a href="/wiki/Intramolecular_reaction" title="Intramolecular reaction">intramolecularly</a> blocks its activity as a protective mechanism against uncontrolled catalysis. The N‑terminal peptide is cleaved (split) from the zymogen enzyme precursor by another enzyme to release an active enzyme.<a href="#cite_note-Boon_2020-8">[8]</a> The <a href="/wiki/Binding_site" title="Binding site">binding site</a> of inhibitors on enzymes is most commonly the same site that binds the <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> of the enzyme. These <a href="/wiki/Active_site" title="Active site">active site</a> inhibitors are known as <a href="/wiki/Allosteric_regulation#Allosteric_sites_as_drug_targets" title="Allosteric regulation">orthosteric</a> ("regular" orientation) inhibitors.<a href="#cite_note-Rydzewski_2010-9">[9]</a> The mechanism of orthosteric inhibition is simply to prevent substrate binding to the enzyme through direct competition which in turn prevents the enzyme from catalysing the conversion of substrates into products. Alternatively, the inhibitor can bind to a site remote from the enzyme active site. These are known as <a href="/wiki/Allosteric_inhibitor" class="mw-redirect" title="Allosteric inhibitor">allosteric</a> ("alternative" orientation) inhibitors.<a href="#cite_note-Rydzewski_2010-9">[9]</a> The mechanisms of allosteric inhibition are varied and include changing the <a href="/wiki/Conformational_isomerism" class="mw-redirect" title="Conformational isomerism">conformation</a> (shape) of the enzyme such that it can no longer bind substrate (<a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">kinetically</a> indistinguishable from competitive orthosteric inhibition)<a href="#cite_note-pmid30917186-10">[10]</a> or alternatively stabilise binding of substrate to the enzyme but lock the enzyme in a conformation which is no longer catalytically active.<a href="#cite_note-Patrick_2013-11">[11]</a> <div class="mw-heading mw-heading2"><h2 id="Reversible_inhibitors">Reversible inhibitors</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=2" title="Edit section: Reversible inhibitors">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1273380762/mw-parser-output/.tmulti">.mw-parser-output .tmulti .multiimageinner{display:flex;flex-direction:column}.mw-parser-output .tmulti .trow{display:flex;flex-direction:row;clear:left;flex-wrap:wrap;width:100%;box-sizing:border-box}.mw-parser-output .tmulti .tsingle{margin:1px;float:left}.mw-parser-output .tmulti .theader{clear:both;font-weight:bold;text-align:center;align-self:center;background-color:transparent;width:100%}.mw-parser-output .tmulti .thumbcaption{background-color:transparent}.mw-parser-output .tmulti .text-align-left{text-align:left}.mw-parser-output .tmulti .text-align-right{text-align:right}.mw-parser-output .tmulti .text-align-center{text-align:center}@media all and (max-width:720px){.mw-parser-output .tmulti .thumbinner{width:100%!important;box-sizing:border-box;max-width:none!important;align-items:center}.mw-parser-output .tmulti .trow{justify-content:center}.mw-parser-output .tmulti .tsingle{float:none!important;max-width:100%!important;box-sizing:border-box;text-align:center}.mw-parser-output .tmulti .tsingle .thumbcaption{text-align:left}.mw-parser-output .tmulti .trow>.thumbcaption{text-align:center}}@media screen{html.skin-theme-clientpref-night .mw-parser-output .tmulti .multiimageinner span:not(.skin-invert-image):not(.skin-invert):not(.bg-transparent) img{background-color:white}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .tmulti .multiimageinner span:not(.skin-invert-image):not(.skin-invert):not(.bg-transparent) img{background-color:white}}</style><div class="thumb tmulti tright"><div class="thumbinner multiimageinner" style="width:408px;max-width:408px"><div class="trow"><div class="theader">Inhibition mechanism schematic</div></div><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Inhibition_mechanism_(reversible).svg" class="mw-file-description"><img alt="chemical equilibrium reaction formula for competitive, uncompetitive, non-competitive, and mixed inhibition" src="//upload.wikimedia.org/wikipedia/commons/thumb/8/8d/Inhibition_mechanism_%28reversible%29.svg/250px-Inhibition_mechanism_%28reversible%29.svg.png" decoding="async" width="200" height="462" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/8d/Inhibition_mechanism_%28reversible%29.svg/330px-Inhibition_mechanism_%28reversible%29.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/8d/Inhibition_mechanism_%28reversible%29.svg/500px-Inhibition_mechanism_%28reversible%29.svg.png 2x" data-file-width="1300" data-file-height="3000" /></a></div><div class="thumbcaption">Kinetic mechanisms for reversible inhibition. Substrate (S) binding to enzyme (E) in blue, catalysis releasing product (P) in red, inhibitor (I) binding to enzyme in green.</div></div><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Inhibition_schematic_(reversible).svg" class="mw-file-description"><img alt="schematic diagram of the three types of reversible inhibitors" src="//upload.wikimedia.org/wikipedia/commons/thumb/b/b8/Inhibition_schematic_%28reversible%29.svg/250px-Inhibition_schematic_%28reversible%29.svg.png" decoding="async" width="200" height="489" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/b8/Inhibition_schematic_%28reversible%29.svg/330px-Inhibition_schematic_%28reversible%29.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/b8/Inhibition_schematic_%28reversible%29.svg/500px-Inhibition_schematic_%28reversible%29.svg.png 2x" data-file-width="1800" data-file-height="4400" /></a></div><div class="thumbcaption">Schematics for reversible inhibition. Binding site in blue, substrate in black, inhibitor in green, and allosteric site in light green.</div></div></div><div class="trow" style="display:flex"><div class="thumbcaption">Competitive inhibitors usually bind to the active site. Non-competitive bind to a remote (allosteric) site. Uncompetitive inhibitors only bind once the substrate is bound, fully disrupting catalysis, and mixed inhibition is similar but with only partial disruption of catalysis.</div></div></div></div> Reversible inhibitors attach to enzymes with <a href="/wiki/Non-covalent_interaction" title="Non-covalent interaction">non-covalent interactions</a> such as <a href="/wiki/Hydrogen_bond" title="Hydrogen bond">hydrogen bonds</a>, <a href="/wiki/Hydrophobic_interaction" class="mw-redirect" title="Hydrophobic interaction">hydrophobic interactions</a> and <a href="/wiki/Ionic_bond" class="mw-redirect" title="Ionic bond">ionic bonds</a>.<a href="#cite_note-12">[12]</a> Multiple weak bonds between the inhibitor and the enzyme <a href="/wiki/Active_site" title="Active site">active site</a> combine to produce strong and specific binding. In contrast to irreversible inhibitors, reversible inhibitors generally do not undergo chemical reactions when bound to the enzyme and can be easily removed by dilution or <a href="/wiki/Kidney_dialysis" title="Kidney dialysis">dialysis</a>. A special case is covalent reversible inhibitors that form a chemical bond with the enzyme, but the bond can be cleaved so the inhibition is fully reversible.<a href="#cite_note-Tuley_2018-13">[13]</a> Reversible inhibitors are generally categorized into four types, as introduced by <a href="/wiki/W._Wallace_Cleland" title="W. Wallace Cleland">Cleland</a> in 1963.<a href="#cite_note-Cleland_1963-14">[14]</a> They are classified according to the effect of the inhibitor on the Vmax (maximum reaction rate catalysed by the enzyme) and Km (the concentration of substrate resulting in half maximal enzyme activity) as the concentration of the enzyme's substrate is varied.<a href="#cite_note-15">[15]</a><a href="#cite_note-NIH_CTT-16">[16]</a> <div class="mw-heading mw-heading3"><h3 id="Competitive">Competitive</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=3" title="Edit section: Competitive">edit</a>]</div> In <a href="/wiki/Competitive_inhibition" title="Competitive inhibition">competitive inhibition</a> the substrate and inhibitor cannot bind to the enzyme at the same time.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 134  This usually results from the inhibitor having an affinity for the active site of an enzyme where the substrate also binds; the substrate and inhibitor compete for access to the enzyme's active site. This type of inhibition can be overcome by sufficiently high concentrations of substrate (Vmax remains constant), i.e., by out-competing the inhibitor.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 134–135  However, the apparent Km will increase as it takes a higher concentration of the substrate to reach the Km point, or half the Vmax. Competitive inhibitors are often similar in structure to the real substrate (see for example the "methotrexate versus folate" figure in the <a href="#Drugs">"Drugs" section</a>).<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 134  <div class="mw-heading mw-heading3"><h3 id="Uncompetitive">Uncompetitive</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=4" title="Edit section: Uncompetitive">edit</a>]</div> In <a href="/wiki/Uncompetitive_inhibition" title="Uncompetitive inhibition">uncompetitive inhibition</a> the inhibitor binds only to the enzyme-substrate complex.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 139  This type of inhibition causes Vmax to decrease (maximum velocity decreases as a result of removing activated complex) and Km to decrease (due to better binding efficiency as a result of <a href="/wiki/Le_Chatelier%27s_principle" title="Le Chatelier's principle">Le Chatelier's principle</a> and the effective elimination of the ES complex thus decreasing the Km which indicates a higher binding affinity).<a href="#cite_note-Segel-18">[18]</a> Uncompetitive inhibition is rare.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 139 <a href="#cite_note-Palmer_2007-19">[19]</a> <div class="mw-heading mw-heading3"><h3 id="Non-competitive">Non-competitive</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=5" title="Edit section: Non-competitive">edit</a>]</div> In <a href="/wiki/Non-competitive_inhibition" title="Non-competitive inhibition">non-competitive inhibition</a> the binding of the inhibitor to the enzyme reduces its <a href="/wiki/Enzyme_activity" class="mw-redirect" title="Enzyme activity">activity</a> but does not affect the binding of substrate.<a href="#cite_note-NIH_CTT-16">[16]</a> This type of inhibitor binds with equal affinity to the free enzyme as to the enzyme-substrate complex. It can be thought of as having the ability of competitive and uncompetitive inhibitors, but with no preference to either type. As a result, the extent of inhibition depends only on the concentration of the inhibitor. Vmax will decrease due to the inability for the reaction to proceed as efficiently, but Km will remain the same as the actual binding of the substrate, by definition, will still function properly.<a href="#cite_note-Delaune_2021-20">[20]</a> <div class="mw-heading mw-heading3"><h3 id="Mixed">Mixed</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=6" title="Edit section: Mixed">edit</a>]</div> In <a href="/wiki/Mixed_inhibition" title="Mixed inhibition">mixed inhibition</a> the inhibitor may bind to the enzyme whether or not the substrate has already bound. Hence mixed inhibition is a combination of competitive and noncompetitive inhibition.<a href="#cite_note-NIH_CTT-16">[16]</a> Furthermore, the affinity of the inhibitor for the free enzyme and the enzyme-substrate complex may differ.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 136–139  By increasing concentrations of substrate [S], this type of inhibition can be reduced (due to the competitive contribution), but not entirely overcome (due to the noncompetitive component).<a href="#cite_note-Voet_2016-21">[21]</a>: 381–382  Although it is possible for mixed-type inhibitors to bind in the active site, this type of inhibition generally results from an <a href="/wiki/Allosteric" class="mw-redirect" title="Allosteric">allosteric</a> effect where the inhibitor binds to a different site on an enzyme. Inhibitor binding to this <a href="/wiki/Allosteric_site" class="mw-redirect" title="Allosteric site">allosteric site</a> changes the <a href="/wiki/Conformational_isomerism" class="mw-redirect" title="Conformational isomerism">conformation</a> (that is, the <a href="/wiki/Tertiary_structure" class="mw-redirect" title="Tertiary structure">tertiary structure</a> or three-dimensional shape) of the enzyme so that the affinity of the substrate for the active site is reduced.<a href="#cite_note-Buker_2019-22">[22]</a> These four types of inhibition can also be distinguished by the effect of increasing the substrate concentration [S] on the degree of inhibition caused by a given amount of inhibitor. For competitive inhibition the degree of inhibition is reduced by increasing [S], for noncompetitive inhibition the degree of inhibition is unchanged, and for uncompetitive (also called anticompetitive) inhibition the degree of inhibition increases with [S].<a href="#cite_note-23">[23]</a> <div class="mw-heading mw-heading3"><h3 id="Quantitative_description">Quantitative description</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=7" title="Edit section: Quantitative description">edit</a>]</div> Reversible inhibition can be described quantitatively in terms of the inhibitor's <a href="/wiki/Dissociation_constant" title="Dissociation constant">binding</a> to the enzyme and to the enzyme-substrate complex, and its effects on the <a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">kinetic constants</a> of the enzyme.<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 6  In the classic <a href="/wiki/Michaelis-Menten_kinetics" class="mw-redirect" title="Michaelis-Menten kinetics">Michaelis-Menten</a> scheme (shown in the "inhibition mechanism schematic" diagram), an enzyme (E) binds to its substrate (S) to form the enzyme–substrate complex ES. Upon catalysis, this complex breaks down to release product P and free enzyme.<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 55  The inhibitor (I) can bind to either E or ES with the <a href="/wiki/Dissociation_constant" title="Dissociation constant">dissociation constants</a> Ki or Ki', respectively.<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 87  <ul><li>Competitive inhibitors can bind to E, but not to ES. Competitive inhibition increases Km (i.e., the inhibitor interferes with substrate binding), but does not affect Vmax (the inhibitor does not hamper catalysis in ES because it cannot bind to ES).<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 102 </li> <li>Uncompetitive inhibitors bind to ES. Uncompetitive inhibition decreases both Km and Vmax. The inhibitor affects substrate binding by increasing the enzyme's affinity for the substrate (decreasing Km) as well as hampering catalysis (decreases Vmax).<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 106 </li> <li>Non-competitive inhibitors have identical affinities for E and ES (Ki = Ki'). Non-competitive inhibition does not change Km (i.e., it does not affect substrate binding) but decreases Vmax (i.e., inhibitor binding hampers catalysis).<a href="#cite_note-Bisswanger_2017-24">[24]</a>: 97 </li> <li>Mixed-type inhibitors bind to both E and ES, but their affinities for these two forms of the enzyme are different (Ki ≠ Ki'). Thus, mixed-type inhibitors affect substrate binding (increase or decrease Km) and hamper catalysis in the ES complex (decrease Vmax).<a href="#cite_note-Marangoni_2003-25">[25]</a>: 63–64 </li></ul> When an enzyme has multiple substrates, inhibitors can show different types of inhibition depending on which substrate is considered. This results from the active site containing two different binding sites within the active site, one for each substrate. For example, an inhibitor might compete with substrate A for the first binding site, but be a non-competitive inhibitor with respect to substrate B in the second binding site.<a href="#cite_note-26">[26]</a> Traditionally reversible enzyme inhibitors have been classified as competitive, uncompetitive, or non-competitive, according to their effects on Km and Vmax.<a href="#cite_note-Cleland_1963-14">[14]</a> These three types of inhibition result respectively from the inhibitor binding only to the enzyme E in the absence of substrate S, to the enzyme–substrate complex ES, or to both. The division of these classes arises from a problem in their derivation and results in the need to use two different binding constants for one binding event.<a href="#cite_note-Walsh_2021-27">[27]</a> It is further assumed that binding of the inhibitor to the enzyme results in 100% inhibition and fails to consider the possibility of partial inhibition.<a href="#cite_note-Walsh_2021-27">[27]</a> The common form of the inhibitory term also obscures the relationship between the inhibitor binding to the enzyme and its relationship to any other binding term be it the Michaelis–Menten equation or a dose response curve associated with ligand receptor binding. To demonstrate the relationship the following rearrangement can be made:<a href="#cite_note-Walsh_2007-28">[28]</a> <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\begin{aligned}{\cfrac {V_{\max }}{1+{\cfrac {\ce {[I]}}{K_{i}}}}}&={V_{\max }}\left({\cfrac {K_{i}}{K_{i}+[{\ce {I}}]}}\right)&&{\text{multiply by }}{\cfrac {K_{i}}{K_{i}}}=1\\&={V_{\max }}\left({\cfrac {K_{i}+[{\ce {I}}]-[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{add }}[{\ce {I}}]-[{\ce {I}}]=0{\text{ to numerator}}\\&={V_{\max }}\left(1-{\cfrac {[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{simplify }}{\cfrac {K_{i}+[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}=1\\&=V_{\max }-V_{\max }{\cfrac {\ce {[I]}}{K_{i}+[{\ce {I}}]}}&&{\text{multiply out by }}V_{\max }\end{aligned}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mtable columnalign="right left right left right left right left right left right left" rowspacing="3pt" columnspacing="0em 2em 0em 2em 0em 2em 0em 2em 0em 2em 0em" displaystyle="true"> <mtr> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mn>1</mn> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>I</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mtd> <mtd> <mi></mi> <mo>=</mo> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> </mrow> <mrow> <mo>(</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> </mfrac> </mrow> <mo>)</mo> </mrow> </mtd> <mtd></mtd> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mtext>multiply by </mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> <mo>=</mo> <mn>1</mn> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>=</mo> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> </mrow> <mrow> <mo>(</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>−</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> </mfrac> </mrow> <mo>)</mo> </mrow> </mtd> <mtd></mtd> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mtext>add </mtext> </mrow> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>−</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>=</mo> <mn>0</mn> <mrow class="MJX-TeXAtom-ORD"> <mtext> to numerator</mtext> </mrow> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>=</mo> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> </mrow> <mrow> <mo>(</mo> <mrow> <mn>1</mn> <mo>−</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mrow> <mo>)</mo> </mrow> </mtd> <mtd></mtd> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mtext>simplify </mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> </mfrac> </mrow> <mo>=</mo> <mn>1</mn> </mtd> </mtr> <mtr> <mtd></mtd> <mtd> <mi></mi> <mo>=</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> <mo>−</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>I</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mtd> <mtd></mtd> <mtd> <mrow class="MJX-TeXAtom-ORD"> <mtext>multiply out by </mtext> </mrow> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> </mtd> </mtr> </mtable> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\begin{aligned}{\cfrac {V_{\max }}{1+{\cfrac {\ce {[I]}}{K_{i}}}}}&={V_{\max }}\left({\cfrac {K_{i}}{K_{i}+[{\ce {I}}]}}\right)&&{\text{multiply by }}{\cfrac {K_{i}}{K_{i}}}=1\\&={V_{\max }}\left({\cfrac {K_{i}+[{\ce {I}}]-[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{add }}[{\ce {I}}]-[{\ce {I}}]=0{\text{ to numerator}}\\&={V_{\max }}\left(1-{\cfrac {[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{simplify }}{\cfrac {K_{i}+[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}=1\\&=V_{\max }-V_{\max }{\cfrac {\ce {[I]}}{K_{i}+[{\ce {I}}]}}&&{\text{multiply out by }}V_{\max }\end{aligned}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/37eda4dec307f8acfca89b2d8f4811474ea764ec" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -16.171ex; width:68.744ex; height:33.509ex;" alt="{\displaystyle {\begin{aligned}{\cfrac {V_{\max }}{1+{\cfrac {\ce {[I]}}{K_{i}}}}}&={V_{\max }}\left({\cfrac {K_{i}}{K_{i}+[{\ce {I}}]}}\right)&&{\text{multiply by }}{\cfrac {K_{i}}{K_{i}}}=1\\&={V_{\max }}\left({\cfrac {K_{i}+[{\ce {I}}]-[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{add }}[{\ce {I}}]-[{\ce {I}}]=0{\text{ to numerator}}\\&={V_{\max }}\left(1-{\cfrac {[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}\right)&&{\text{simplify }}{\cfrac {K_{i}+[{\ce {I}}]}{K_{i}+[{\ce {I}}]}}=1\\&=V_{\max }-V_{\max }{\cfrac {\ce {[I]}}{K_{i}+[{\ce {I}}]}}&&{\text{multiply out by }}V_{\max }\end{aligned}}}" /></dd></dl> This rearrangement demonstrates that similar to the Michaelis–Menten equation, the maximal rate of reaction depends on the proportion of the enzyme population interacting with its substrate. fraction of the enzyme population bound by substrate <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\cfrac {\ce {[S]}}{[{\ce {S}}]+K_{m}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>S</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>S</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\cfrac {\ce {[S]}}{[{\ce {S}}]+K_{m}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/eb08dd139085a394e6e7370f47ebfa255f1ad685" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:9.911ex; height:7.176ex;" alt="{\displaystyle {\cfrac {\ce {[S]}}{[{\ce {S}}]+K_{m}}}}" /></dd></dl> fraction of the enzyme population bound by inhibitor <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>I</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/9ed50a1f7a5f2c52f406b52263916ab48b268e07" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:8.583ex; height:7.176ex;" alt="{\displaystyle {\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}" /></dd></dl> the effect of the inhibitor is a result of the percent of the enzyme population interacting with inhibitor. The only problem with this equation in its present form is that it assumes absolute inhibition of the enzyme with inhibitor binding, when in fact there can be a wide range of effects anywhere from 100% inhibition of substrate turn over to no inhibition. To account for this the equation can be easily modified to allow for different degrees of inhibition by including a delta Vmax term.<a href="#cite_note-Walsh_2012-29">[29]</a>: 361  <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle V_{\max }-\Delta V_{\max }{\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> <mo>−</mo> <mi mathvariant="normal">Δ</mi> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> </mrow> </msub> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>I</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle V_{\max }-\Delta V_{\max }{\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/7dff424ec79284c3a1cea14f0f82b0eaace53c69" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:22.651ex; height:7.176ex;" alt="{\displaystyle V_{\max }-\Delta V_{\max }{\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}" /></dd></dl> or <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>1</mn> </mrow> </msub> <mo>−</mo> <mo stretchy="false">(</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>1</mn> </mrow> </msub> <mo>−</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>2</mn> </mrow> </msub> <mo stretchy="false">)</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>I</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>I</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/f3874623edd9524ba2741fe448927bf5cf0ab257" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:33.639ex; height:7.176ex;" alt="{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[I]}}{[{\ce {I}}]+K_{i}}}}" /></dd></dl> This term can then define the residual enzymatic activity present when the inhibitor is interacting with individual enzymes in the population. However the inclusion of this term has the added value of allowing for the possibility of activation if the secondary Vmax term turns out to be higher than the initial term. To account for the possibly of activation as well the notation can then be rewritten replacing the inhibitor "I" with a modifier term (stimulator or inhibitor) denoted here as "X".<a href="#cite_note-Walsh_2007-28">[28]</a>: eq 13  <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>1</mn> </mrow> </msub> <mo>−</mo> <mo stretchy="false">(</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>1</mn> </mrow> </msub> <mo>−</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mo movablelimits="true" form="prefix">max</mo> <mn>2</mn> </mrow> </msub> <mo stretchy="false">)</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>X</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>X</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>x</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/306d44733a89308883053e3b8372a8cf9ce0239b" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:34.915ex; height:7.176ex;" alt="{\displaystyle V_{\max 1}-(V_{\max 1}-V_{\max 2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}" /></dd></dl> While this terminology results in a simplified way of dealing with kinetic effects relating to the maximum velocity of the Michaelis–Menten equation, it highlights potential problems with the term used to describe effects relating to the Km. The Km relating to the affinity of the enzyme for the substrate should in most cases relate to potential changes in the binding site of the enzyme which would directly result from enzyme inhibitor interactions. As such a term similar to the delta Vmax term proposed above to modulate Vmax should be appropriate in most situations:<a href="#cite_note-Walsh_2007-28">[28]</a>: eq 14  <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle K_{m1}-(K_{m1}-K_{m2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> <mn>1</mn> </mrow> </msub> <mo>−</mo> <mo stretchy="false">(</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> <mn>1</mn> </mrow> </msub> <mo>−</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> <mn>2</mn> </mrow> </msub> <mo stretchy="false">)</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mtext>X</mtext> <mo stretchy="false">]</mo> </mrow> </mrow> </mstyle> </mrow> <mrow> <mpadded width="0" height="8.6pt" depth="3pt"> <mrow></mrow> </mpadded> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">[</mo> <mrow class="MJX-TeXAtom-ORD"> <mtext>X</mtext> </mrow> <mo stretchy="false">]</mo> <mo>+</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>x</mi> </mrow> </msub> </mrow> </mstyle> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle K_{m1}-(K_{m1}-K_{m2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/cb4e0de216e1e625bb803ee725bf85c9989a15f5" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -3.005ex; width:30.759ex; height:7.176ex;" alt="{\displaystyle K_{m1}-(K_{m1}-K_{m2}){\cfrac {\ce {[X]}}{[{\ce {X}}]+K_{x}}}}" /></dd></dl> <div class="mw-heading mw-heading3"><h3 id="Dissociation_constants">Dissociation constants</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=8" title="Edit section: Dissociation constants">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Inhibition_diagrams-1-.png" class="mw-file-description"><img alt="2D plots of 1/[S] concentration (x-axis) and 1/V (y-axis) demonstrating that as inhibitor concentration is changed, competitive inhibitor lines intersect at a single point on the y-axis, non-competitive inhibitors intersect at the x-axis, and mixed inhibitors intersect a point that is on neither axis" src="//upload.wikimedia.org/wikipedia/commons/thumb/b/ba/Inhibition_diagrams-1-.png/220px-Inhibition_diagrams-1-.png" decoding="async" width="220" height="514" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/b/ba/Inhibition_diagrams-1-.png 1.5x" data-file-width="257" data-file-height="600" /></a><figcaption>Lineweaver–Burk diagrams of different types of reversible enzyme inhibitors. The arrow shows the effect of increasing concentrations of inhibitor.</figcaption></figure> An enzyme inhibitor is characterised by its <a href="/wiki/Dissociation_constant" title="Dissociation constant">dissociation constant</a> Ki, the concentration at which the inhibitor half occupies the enzyme. In non-competitive inhibition the inhibitor can also bind to the enzyme-substrate complex, and the presence of bound substrate can change the affinity of the inhibitor for the enzyme, resulting in a second dissociation constant Ki'. Hence Ki and Ki' are the dissociation constants of the inhibitor for the enzyme and to the enzyme-substrate complex, respectively.<a href="#cite_note-Strelow_2012-30">[30]</a>: Glossary  The enzyme-inhibitor constant Ki can be measured directly by various methods; one especially accurate method is <a href="/wiki/Isothermal_Titration_Calorimetry" class="mw-redirect" title="Isothermal Titration Calorimetry">isothermal titration calorimetry</a>, in which the inhibitor is titrated into a solution of enzyme and the heat released or absorbed is measured.<a href="#cite_note-31">[31]</a> However, the other dissociation constant Ki' is difficult to measure directly, since the enzyme-substrate complex is short-lived and undergoing a chemical reaction to form the product. Hence, Ki' is usually measured indirectly, by observing the <a href="/wiki/Enzyme_activity" class="mw-redirect" title="Enzyme activity">enzyme activity</a> under various substrate and inhibitor concentrations, and fitting the data via <a href="/wiki/Nonlinear_regression" title="Nonlinear regression">nonlinear regression</a><a href="#cite_note-32">[32]</a> to a modified <a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Michaelis–Menten equation</a>.<a href="#cite_note-Voet_2016-21">[21]</a> <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle V={\frac {V_{max}[S]}{\alpha K_{m}+\alpha ^{\prime }[S]}}={\frac {(1/\alpha ^{\prime })V_{max}[S]}{(\alpha /\alpha ^{\prime })K_{m}+[S]}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>V</mi> <mo>=</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> <mi>a</mi> <mi>x</mi> </mrow> </msub> <mo stretchy="false">[</mo> <mi>S</mi> <mo stretchy="false">]</mo> </mrow> <mrow> <mi>α</mi> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> </mrow> </msub> <mo>+</mo> <msup> <mi>α</mi> <mrow class="MJX-TeXAtom-ORD"> <mi class="MJX-variant" mathvariant="normal">′</mi> </mrow> </msup> <mo stretchy="false">[</mo> <mi>S</mi> <mo stretchy="false">]</mo> </mrow> </mfrac> </mrow> <mo>=</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mo stretchy="false">(</mo> <mn>1</mn> <mrow class="MJX-TeXAtom-ORD"> <mo>/</mo> </mrow> <msup> <mi>α</mi> <mrow class="MJX-TeXAtom-ORD"> <mi class="MJX-variant" mathvariant="normal">′</mi> </mrow> </msup> <mo stretchy="false">)</mo> <msub> <mi>V</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> <mi>a</mi> <mi>x</mi> </mrow> </msub> <mo stretchy="false">[</mo> <mi>S</mi> <mo stretchy="false">]</mo> </mrow> <mrow> <mo stretchy="false">(</mo> <mi>α</mi> <mrow class="MJX-TeXAtom-ORD"> <mo>/</mo> </mrow> <msup> <mi>α</mi> <mrow class="MJX-TeXAtom-ORD"> <mi class="MJX-variant" mathvariant="normal">′</mi> </mrow> </msup> <mo stretchy="false">)</mo> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>m</mi> </mrow> </msub> <mo>+</mo> <mo stretchy="false">[</mo> <mi>S</mi> <mo stretchy="false">]</mo> </mrow> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle V={\frac {V_{max}[S]}{\alpha K_{m}+\alpha ^{\prime }[S]}}={\frac {(1/\alpha ^{\prime })V_{max}[S]}{(\alpha /\alpha ^{\prime })K_{m}+[S]}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/4a8f0a9dda1d308de7f090f99c2833f944f11a09" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -2.671ex; width:38.511ex; height:6.509ex;" alt="{\displaystyle V={\frac {V_{max}[S]}{\alpha K_{m}+\alpha ^{\prime }[S]}}={\frac {(1/\alpha ^{\prime })V_{max}[S]}{(\alpha /\alpha ^{\prime })K_{m}+[S]}}}" /></dd></dl> where the modifying factors α and α' are defined by the inhibitor concentration and its two dissociation constants <dl><dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle \alpha =1+{\frac {[I]}{K_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mi>α</mi> <mo>=</mo> <mn>1</mn> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mo stretchy="false">[</mo> <mi>I</mi> <mo stretchy="false">]</mo> </mrow> <msub> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> </msub> </mfrac> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle \alpha =1+{\frac {[I]}{K_{i}}}}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/57fcf54938a9784f9313437681b220079ff43ee5" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -2.338ex; width:12.198ex; height:6.176ex;" alt="{\displaystyle \alpha =1+{\frac {[I]}{K_{i}}}}" /></dd> <dd><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle \alpha ^{\prime }=1+{\frac {[I]}{K_{i}^{\prime }}}.}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <msup> <mi>α</mi> <mrow class="MJX-TeXAtom-ORD"> <mi class="MJX-variant" mathvariant="normal">′</mi> </mrow> </msup> <mo>=</mo> <mn>1</mn> <mo>+</mo> <mrow class="MJX-TeXAtom-ORD"> <mfrac> <mrow> <mo stretchy="false">[</mo> <mi>I</mi> <mo stretchy="false">]</mo> </mrow> <msubsup> <mi>K</mi> <mrow class="MJX-TeXAtom-ORD"> <mi>i</mi> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mi class="MJX-variant" mathvariant="normal">′</mi> </mrow> </msubsup> </mfrac> </mrow> <mo>.</mo> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle \alpha ^{\prime }=1+{\frac {[I]}{K_{i}^{\prime }}}.}</annotation> </semantics> </math><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/65bf16742482cae7b0743781f47c327ddcf537e3" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -2.671ex; width:13.535ex; height:6.509ex;" alt="{\displaystyle \alpha ^{\prime }=1+{\frac {[I]}{K_{i}^{\prime }}}.}" /></dd></dl> Thus, in the presence of the inhibitor, the enzyme's effective Km and Vmax become (α/α')Km and (1/α')Vmax, respectively. However, the modified Michaelis-Menten equation assumes that binding of the inhibitor to the enzyme has reached equilibrium, which may be a very slow process for inhibitors with sub-nanomolar dissociation constants. In these cases the inhibition becomes effectively irreversible, hence it is more practical to treat such tight-binding inhibitors as irreversible (see <a href="#Irreversible_inhibitors">below</a>). The effects of different types of reversible enzyme inhibitors on enzymatic activity can be visualised using graphical representations of the Michaelis–Menten equation, such as <a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk</a>, <a href="/wiki/Eadie-Hofstee_diagram" class="mw-redirect" title="Eadie-Hofstee diagram">Eadie-Hofstee</a> or <a href="/wiki/Hanes-Woolf_plot" class="mw-redirect" title="Hanes-Woolf plot">Hanes-Woolf plots</a>.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 140–144  An illustration is provided by the three Lineweaver–Burk plots depicted in the Lineweaver–Burk diagrams figure. In the top diagram the competitive inhibition lines intersect on the y-axis, illustrating that such inhibitors do not affect Vmax. In the bottom diagram the non-competitive inhibition lines intersect on the x-axis, showing these inhibitors do not affect Km. However, since it can be difficult to estimate Ki and Ki' accurately from such plots,<a href="#cite_note-Tseng_1990-33">[33]</a> it is advisable to estimate these constants using more reliable nonlinear regression methods.<a href="#cite_note-Tseng_1990-33">[33]</a> <div class="mw-heading mw-heading3"><h3 id="Special_cases">Special cases</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=9" title="Edit section: Special cases">edit</a>]</div> <div class="mw-heading mw-heading4"><h4 id="Partially_competitive">Partially competitive</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=10" title="Edit section: Partially competitive">edit</a>]</div> The mechanism of partially competitive inhibition is similar to that of non-competitive, except that the EIS complex has catalytic activity, which may be lower or even higher (partially competitive activation) than that of the enzyme–substrate (ES) complex. This inhibition typically displays a lower Vmax, but an unaffected Km value.<a href="#cite_note-Segel-18">[18]</a> <div class="mw-heading mw-heading4"><h4 id="Substrate_or_product">Substrate or product</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=11" title="Edit section: Substrate or product">edit</a>]</div> Substrate or product inhibition is where either an enzymes substrate or product also act as an inhibitor. This inhibition may follow the competitive, uncompetitive or mixed patterns. In substrate inhibition there is a progressive decrease in activity at high substrate concentrations, potentially from an enzyme having two competing substrate-binding sites. At low substrate, the high-affinity site is occupied and normal <a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">kinetics</a> are followed. However, at higher concentrations, the second inhibitory site becomes occupied, inhibiting the enzyme.<a href="#cite_note-34">[34]</a> Product inhibition (either the enzyme's own product, or a product to an enzyme downstream in its metabolic pathway) is often a <a href="#Metabolic_regulation">regulatory feature in metabolism</a> and can be a form of <a href="/wiki/Negative_feedback" title="Negative feedback">negative feedback</a>.<a href="#cite_note-Sauro_2017-2">[2]</a> <div class="mw-heading mw-heading4"><h4 id="Slow-tight">Slow-tight</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=12" title="Edit section: Slow-tight">edit</a>]</div> Slow-tight inhibition occurs when the initial enzyme–inhibitor complex EI undergoes <a href="/wiki/Conformational_isomerism" class="mw-redirect" title="Conformational isomerism">conformational isomerism</a> (a change in shape) to a second more tightly held complex, EI*, but the overall inhibition process is reversible. This manifests itself as slowly increasing enzyme inhibition. Under these conditions, traditional Michaelis–Menten kinetics give a false value for Ki, which is time–dependent. The true value of Ki can be obtained through more complex analysis of the on (kon) and off (koff) rate constants for inhibitor association with kinetics similar to <a href="/wiki/Irreversible_inhibition" class="mw-redirect" title="Irreversible inhibition">irreversible inhibition</a>.<a href="#cite_note-Cornish-Bowden_2012-17">[17]</a>: 168  <div class="mw-heading mw-heading4"><h4 id="Multi-substrate_analogues">Multi-substrate analogues</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=13" title="Edit section: Multi-substrate analogues">edit</a>]</div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1273380762/mw-parser-output/.tmulti" /><div class="thumb tmulti tright"><div class="thumbinner multiimageinner" style="width:204px;max-width:204px"><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:TGDDF-GDDF.svg" class="mw-file-description"><img alt="TGDDF / GDDF MAIs where blue depicts the tetrahydrofolate cofactor analogue, black GAR or thioGAR and red, the connecting atoms." src="//upload.wikimedia.org/wikipedia/commons/thumb/3/3f/TGDDF-GDDF.svg/200px-TGDDF-GDDF.svg.png" decoding="async" width="200" height="132" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/3f/TGDDF-GDDF.svg/300px-TGDDF-GDDF.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/3f/TGDDF-GDDF.svg/400px-TGDDF-GDDF.svg.png 2x" data-file-width="328" data-file-height="216" /></a></div><div class="thumbcaption">TGDDF/GDDF multi-substrate adduct inhibitor. Substrate analogue in black, cofactor analogue in blue, non-cleavable linker in red.</div></div></div><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Ritonavir_Schechter_Berger_Notation.svg" class="mw-file-description"><img alt="Ritonavir is similar to the natural substrate." src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e9/Ritonavir_Schechter_Berger_Notation.svg/200px-Ritonavir_Schechter_Berger_Notation.svg.png" decoding="async" width="200" height="108" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e9/Ritonavir_Schechter_Berger_Notation.svg/300px-Ritonavir_Schechter_Berger_Notation.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e9/Ritonavir_Schechter_Berger_Notation.svg/400px-Ritonavir_Schechter_Berger_Notation.svg.png 2x" data-file-width="356" data-file-height="193" /></a></div><div class="thumbcaption">Peptide-based HIV-1 protease inhibitor <a href="/wiki/Ritonavir" title="Ritonavir">ritonavir</a> with substrate binding sites located in enzyme labelled as S2, S1, S1', and S2'.</div></div></div><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Tipranavir_structure_2.svg" class="mw-file-description"><img alt="Tipranavir is not similar to the natural substrate." src="//upload.wikimedia.org/wikipedia/commons/thumb/9/99/Tipranavir_structure_2.svg/250px-Tipranavir_structure_2.svg.png" decoding="async" width="200" height="140" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/99/Tipranavir_structure_2.svg/330px-Tipranavir_structure_2.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/99/Tipranavir_structure_2.svg/500px-Tipranavir_structure_2.svg.png 2x" data-file-width="512" data-file-height="359" /></a></div><div class="thumbcaption">Nonpeptidic HIV-1 protease inhibitor <a href="/wiki/Tipranavir" title="Tipranavir">tipranavir</a></div></div></div></div></div> Multi-substrate analogue inhibitors are high affinity selective inhibitors that can be prepared for enzymes that catalyse reactions with more than one substrate by capturing the binding energy of each of those substrate into one molecule.<a href="#cite_note-35">[35]</a><a href="#cite_note-36">[36]</a> For example, in the <a href="/wiki/Formylation" title="Formylation">formyl transfer</a> reactions of <a href="/wiki/Purine_biosynthesis" class="mw-redirect" title="Purine biosynthesis">purine biosynthesis</a>, a potent Multi-substrate Adduct Inhibitor (MAI) to glycinamide ribonucleotide (GAR) <a href="/wiki/Phosphoribosylglycinamide_formyltransferase" title="Phosphoribosylglycinamide formyltransferase">TFase</a> was prepared synthetically by linking analogues of the GAR substrate and the <a href="/wiki/10-Formyltetrahydrofolate" title="10-Formyltetrahydrofolate">N-10-formyl tetrahydrofolate</a> cofactor together to produce thioglycinamide ribonucleotide dideazafolate (TGDDF),<a href="#cite_note-37">[37]</a> or enzymatically from the natural GAR substrate to yield GDDF.<a href="#cite_note-38">[38]</a> Here the subnanomolar dissociation constant (KD) of TGDDF was greater than predicted presumably due to <a href="/wiki/Entropic" class="mw-redirect" title="Entropic">entropic</a> advantages gained and/or positive interactions acquired through the atoms linking the components. MAIs have also been observed to be produced in cells by reactions of pro-drugs such as <a href="/wiki/Isoniazid" title="Isoniazid">isoniazid</a><a href="#cite_note-39">[39]</a> or enzyme inhibitor ligands (for example, <a href="/wiki/PTC124" class="mw-redirect" title="PTC124">PTC124</a>)<a href="#cite_note-40">[40]</a> with cellular cofactors such as <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">nicotinamide adenine dinucleotide</a> (NADH) and <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">adenosine triphosphate</a> (ATP) respectively.<a href="#cite_note-Le_Calvez_2009-41">[41]</a> <div class="mw-heading mw-heading3"><h3 id="Examples">Examples</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=14" title="Edit section: Examples">edit</a>]</div> As enzymes have evolved to bind their substrates tightly, and most reversible inhibitors bind in the active site of enzymes, it is unsurprising that some of these inhibitors are strikingly similar in structure to the substrates of their targets. Inhibitors of <a href="/wiki/Dihydrofolate_reductase" title="Dihydrofolate reductase">dihydrofolate reductase</a> (DHFR) are prominent examples.<a href="#cite_note-Avendano_2015-42">[42]</a> Other examples of these substrate mimics are the <a href="/wiki/Protease_inhibitors" class="mw-redirect" title="Protease inhibitors">protease inhibitors</a>, a therapeutically effective class of <a href="/wiki/Antiretroviral_drug" class="mw-redirect" title="Antiretroviral drug">antiretroviral drugs</a> used to treat <a href="/wiki/HIV/AIDS" title="HIV/AIDS">HIV/AIDS</a>.<a href="#cite_note-43">[43]</a><a href="#cite_note-Agbowuro_2018-44">[44]</a> The structure of <a href="/wiki/Ritonavir" title="Ritonavir">ritonavir</a>, a <a href="/wiki/Peptidomimetic" title="Peptidomimetic">peptidomimetic</a> (peptide mimic) protease inhibitor containing three <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a>, as shown in the <a href="#Competitive">"competitive inhibition"</a> figure above. As this drug resembles the peptide that is the substrate of the HIV protease, it competes with the substrate in the enzyme's active site.<a href="#cite_note-Qiu_2011-45">[45]</a> Enzyme inhibitors are often designed to mimic the <a href="/wiki/Transition_state" title="Transition state">transition state</a> or intermediate of an enzyme-catalysed reaction.<a href="#cite_note-Schramm_2018-46">[46]</a> This ensures that the inhibitor exploits the transition state stabilising effect of the enzyme, resulting in a better binding affinity (lower Ki) than substrate-based designs. An example of such a transition state inhibitor is the antiviral drug <a href="/wiki/Oseltamivir" title="Oseltamivir">oseltamivir</a>; this drug mimics the planar nature of the ring <a href="/wiki/Oxonium_ion" title="Oxonium ion">oxonium ion</a> in the reaction of the viral enzyme <a href="/wiki/Neuraminidase" title="Neuraminidase">neuraminidase</a>.<a href="#cite_note-pmid10702632-47">[47]</a> However, not all inhibitors are based on the structures of substrates. For example, the structure of another HIV protease inhibitor <a href="/wiki/Tipranavir" title="Tipranavir">tipranavir</a> is not based on a peptide and has no obvious structural similarity to a protein substrate. These non-peptide inhibitors can be more stable than inhibitors containing peptide bonds, because they will not be substrates for <a href="/wiki/Peptidase" class="mw-redirect" title="Peptidase">peptidases</a> and are less likely to be degraded.<a href="#cite_note-48">[48]</a> In drug design it is important to consider the concentrations of substrates to which the target enzymes are exposed. For example, some <a href="/wiki/Protein_kinase" title="Protein kinase">protein kinase</a> inhibitors have chemical structures that are similar to ATP, one of the substrates of these enzymes.<a href="#cite_note-Breen_2015-49">[49]</a> However, drugs that are simple competitive inhibitors will have to compete with the high concentrations of ATP in the cell. Protein kinases can also be inhibited by competition at the binding sites where the kinases interact with their substrate proteins, and most proteins are present inside cells at concentrations much lower than the concentration of ATP. As a consequence, if two protein kinase inhibitors both bind in the active site with similar affinity, but only one has to compete with ATP, then the competitive inhibitor at the protein-binding site will inhibit the enzyme more effectively.<a href="#cite_note-50">[50]</a> <div class="mw-heading mw-heading2"><h2 id="Irreversible_inhibitors">Irreversible inhibitors</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=15" title="Edit section: Irreversible inhibitors">edit</a>]</div> <div class="mw-heading mw-heading3"><h3 id="Types">Types</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=16" title="Edit section: Types">edit</a>]</div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1273380762/mw-parser-output/.tmulti" /><div class="thumb tmulti tright"><div class="thumbinner multiimageinner" style="width:408px;max-width:408px"><div class="trow"><div class="theader">DFP reaction</div></div><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:DIF_reaction.png" class="mw-file-description"><img alt="2D structural diagram depicting a serine amino acid residue from the active site of the enzyme forming a covalent bond with DFP by displacing the fluoride atom" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/23/DIF_reaction.png/200px-DIF_reaction.png" decoding="async" width="200" height="304" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/23/DIF_reaction.png/300px-DIF_reaction.png 1.5x, //upload.wikimedia.org/wikipedia/commons/2/23/DIF_reaction.png 2x" data-file-width="384" data-file-height="583" /></a></div><div class="thumbcaption">Reaction of the irreversible inhibitor <a href="/wiki/Diisopropylfluorophosphate" class="mw-redirect" title="Diisopropylfluorophosphate">diisopropylfluorophosphate</a> (DFP) with a <a href="/wiki/Serine_protease" title="Serine protease">serine protease</a></div></div><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Inhibition_schematic_(irreversible).svg" class="mw-file-description"><img alt="" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Inhibition_schematic_%28irreversible%29.svg/250px-Inhibition_schematic_%28irreversible%29.svg.png" decoding="async" width="200" height="515" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Inhibition_schematic_%28irreversible%29.svg/330px-Inhibition_schematic_%28irreversible%29.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/21/Inhibition_schematic_%28irreversible%29.svg/400px-Inhibition_schematic_%28irreversible%29.svg.png 2x" data-file-width="496" data-file-height="1276" /></a></div><div class="thumbcaption">Irreversible inhibitors bind to the enzyme's binding site then undergo a chemical reaction to form a covalent enzyme-inhibitor complex (EI*). Binding site in blue, inhibitor in green.</div></div></div></div></div> Irreversible inhibitors <a href="/wiki/Covalent" class="mw-redirect" title="Covalent">covalently</a> bind to an enzyme, and this type of inhibition can therefore not be readily reversed.<a href="#cite_note-Patrick_2017-51">[51]</a> Irreversible inhibitors often contain reactive functional groups such as <a href="/wiki/Nitrogen_mustard" title="Nitrogen mustard">nitrogen mustards</a>, <a href="/wiki/Aldehyde" title="Aldehyde">aldehydes</a>, <a href="/wiki/Haloalkane" title="Haloalkane">haloalkanes</a>, <a href="/wiki/Alkene" title="Alkene">alkenes</a>, <a href="/wiki/Michael_acceptor" class="mw-redirect" title="Michael acceptor">Michael acceptors</a>, <a href="/wiki/Sulfonate" title="Sulfonate">phenyl sulfonates</a>, or <a href="/wiki/Methoxy_arachidonyl_fluorophosphonate" title="Methoxy arachidonyl fluorophosphonate">fluorophosphonates</a>.<a href="#cite_note-Gehringer_2019-52">[52]</a> These <a href="/wiki/Electrophilic" class="mw-redirect" title="Electrophilic">electrophilic</a> groups react with amino acid side chains to form covalent <a href="/wiki/Adduct" title="Adduct">adducts</a>.<a href="#cite_note-Patrick_2017-51">[51]</a> The residues modified are those with side chains containing <a href="/wiki/Nucleophile" title="Nucleophile">nucleophiles</a> such as <a href="/wiki/Hydroxyl" class="mw-redirect" title="Hydroxyl">hydroxyl</a> or <a href="/wiki/Sulfhydryl" class="mw-redirect" title="Sulfhydryl">sulfhydryl</a> groups; these include the amino acids <a href="/wiki/Serine" title="Serine">serine</a> (that reacts with <a href="/wiki/Diisopropylfluorophosphate" class="mw-redirect" title="Diisopropylfluorophosphate">DFP</a>, see the "DFP reaction" diagram), and also <a href="/wiki/Cysteine" title="Cysteine">cysteine</a>, <a href="/wiki/Threonine" title="Threonine">threonine</a>, or <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>.<a href="#cite_note-53">[53]</a> Irreversible inhibition is different from irreversible enzyme inactivation.<a href="#cite_note-54">[54]</a> Irreversible inhibitors are generally specific for one class of enzyme and do not inactivate all proteins; they do not function by destroying <a href="/wiki/Protein_structure" title="Protein structure">protein structure</a> but by specifically altering the active site of their target. For example, extremes of pH or temperature usually cause <a href="/wiki/Denaturation_(biochemistry)" title="Denaturation (biochemistry)">denaturation</a> of all protein structure, but this is a non-specific effect. Similarly, some non-specific chemical treatments destroy protein structure: for example, heating in concentrated <a href="/wiki/Hydrochloric_acid" title="Hydrochloric acid">hydrochloric acid</a> will hydrolyse the <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a> holding proteins together, releasing free amino acids.<a href="#cite_note-55">[55]</a> Irreversible inhibitors display time-dependent inhibition and their potency therefore cannot be characterised by an IC50 value. This is because the amount of active enzyme at a given concentration of irreversible inhibitor will be different depending on how long the inhibitor is pre-incubated with the enzyme. Instead, kobs/[I] values are used,<a href="#cite_note-56">[56]</a> where kobs is the observed pseudo-first order rate of inactivation (obtained by plotting the log of % activity versus time) and [I] is the concentration of inhibitor. The kobs/[I] parameter is valid as long as the inhibitor does not saturate binding with the enzyme (in which case kobs = kinact) where kinact is the rate of inactivation. <div class="mw-heading mw-heading3"><h3 id="Measuring">Measuring</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=17" title="Edit section: Measuring">edit</a>]</div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1273380762/mw-parser-output/.tmulti" /><div class="thumb tmulti tright"><div class="thumbinner multiimageinner" style="width:204px;max-width:204px"><div class="trow"><div class="theader">Irreversible inhibition mechanism</div></div><div class="trow"><div class="tsingle" style="width:202px;max-width:202px"><div class="thumbimage"><a href="/wiki/File:Inhibition_mechanism_(irreversible).svg" class="mw-file-description"><img alt="Depiction of the reversible chemical equilibria between enzyme + substrate, enzyme/substrate complex, and enzyme + product, and two competing equilibria. The first is between enzyme + inhibitor, enzyme/inhibitor non-covalent complex, followed by irreversible formation of the covalent complex. The second is between enzyme/substrate complex + inhibitor, noncovalent enzyme/substrate, followed by irreversible formation of the covalent complex" src="//upload.wikimedia.org/wikipedia/commons/thumb/0/02/Inhibition_mechanism_%28irreversible%29.svg/200px-Inhibition_mechanism_%28irreversible%29.svg.png" decoding="async" width="200" height="200" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/02/Inhibition_mechanism_%28irreversible%29.svg/300px-Inhibition_mechanism_%28irreversible%29.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/02/Inhibition_mechanism_%28irreversible%29.svg/400px-Inhibition_mechanism_%28irreversible%29.svg.png 2x" data-file-width="1300" data-file-height="1300" /></a></div><div class="thumbcaption">Kinetic mechanism for irreversible inhibition. Substrate binding in blue, catalysis in red, inhibitor binding in green, inactivation reaction in dark green.</div></div></div></div></div> Irreversible inhibitors first form a reversible non-covalent complex with the enzyme (EI or ESI). Subsequently, a chemical reaction occurs between the enzyme and inhibitor to produce the covalently modified "dead-end complex" EI* (an irreversible covalent complex). The rate at which EI* is formed is called the inactivation rate or kinact.<a href="#cite_note-Tuley_2018-13">[13]</a> Since formation of EI may compete with ES, binding of irreversible inhibitors can be prevented by competition either with substrate or with a second, reversible inhibitor. This protection effect is good evidence of a specific reaction of the irreversible inhibitor with the active site. The binding and inactivation steps of this reaction are investigated by incubating the enzyme with inhibitor and assaying the amount of activity remaining over time. The activity will be decreased in a time-dependent manner, usually following <a href="/wiki/Exponential_decay" title="Exponential decay">exponential decay</a>. Fitting these data to a <a href="/wiki/Rate_equation" title="Rate equation">rate equation</a> gives the rate of inactivation at this concentration of inhibitor. This is done at several different concentrations of inhibitor. If a reversible EI complex is involved the inactivation rate will be saturable and fitting this curve will give kinact and Ki.<a href="#cite_note-57">[57]</a> Another method that is widely used in these analyses is <a href="/wiki/Mass_spectrometry" title="Mass spectrometry">mass spectrometry</a>. Here, accurate measurement of the mass of the unmodified native enzyme and the inactivated enzyme gives the increase in mass caused by reaction with the inhibitor and shows the stoichiometry of the reaction.<a href="#cite_note-pmid10398927-58">[58]</a> This is usually done using a <a href="/wiki/MALDI-TOF" class="mw-redirect" title="MALDI-TOF">MALDI-TOF</a> mass spectrometer.<a href="#cite_note-59">[59]</a> In a complementary technique, <a href="/wiki/Peptide_mass_fingerprinting" title="Peptide mass fingerprinting">peptide mass fingerprinting</a> involves digestion of the native and modified protein with a <a href="/wiki/Protease" title="Protease">protease</a> such as <a href="/wiki/Trypsin" title="Trypsin">trypsin</a>. This will produce a set of <a href="/wiki/Peptide" title="Peptide">peptides</a> that can be analysed using a mass spectrometer. The peptide that changes in mass after reaction with the inhibitor will be the one that contains the site of modification.<a href="#cite_note-Sibille_2012-60">[60]</a> <div class="mw-heading mw-heading3"><h3 id="Slow_binding">Slow binding</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=18" title="Edit section: Slow binding">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:DFMO_inhibitor_mechanism.svg" class="mw-file-description"><img alt="2D chemical structure diagram depicting a lysine residue from the enzyme first reacting with DFMO, elimination of fluoride and carbon dioxide, followed by cysteine attacking the covalent lysine-DFMO adduct freeing the lysine residue to form an irreversible cysteine adduct" src="//upload.wikimedia.org/wikipedia/commons/thumb/c/c4/DFMO_inhibitor_mechanism.svg/250px-DFMO_inhibitor_mechanism.svg.png" decoding="async" width="220" height="109" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/c4/DFMO_inhibitor_mechanism.svg/330px-DFMO_inhibitor_mechanism.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/c4/DFMO_inhibitor_mechanism.svg/500px-DFMO_inhibitor_mechanism.svg.png 2x" data-file-width="528" data-file-height="262" /></a><figcaption>Chemical mechanism for irreversible inhibition of ornithine decarboxylase by DFMO. Pyridoxal 5'-phosphate (Py) and enzyme (E) are not shown. Adapted from Poulin et al, 1992.<a href="#cite_note-Poulin-61">[61]</a></figcaption></figure> Not all irreversible inhibitors form covalent adducts with their enzyme targets. Some reversible inhibitors bind so tightly to their target enzyme that they are essentially irreversible. These tight-binding inhibitors may show kinetics similar to covalent irreversible inhibitors. In these cases some of these inhibitors rapidly bind to the enzyme in a low-affinity EI complex and this then undergoes a slower rearrangement to a very tightly bound EI* complex (see the "irreversible inhibition mechanism" diagram). This kinetic behaviour is called slow-binding.<a href="#cite_note-62">[62]</a> This slow rearrangement after binding often involves a <a href="/wiki/Conformational_change" title="Conformational change">conformational change</a> as the enzyme "clamps down" around the inhibitor molecule. Examples of slow-binding inhibitors include some important drugs, such <a href="/wiki/Methotrexate" title="Methotrexate">methotrexate</a>,<a href="#cite_note-63">[63]</a> <a href="/wiki/Allopurinol" title="Allopurinol">allopurinol</a>,<a href="#cite_note-64">[64]</a> and the activated form of <a href="/wiki/Acyclovir" class="mw-redirect" title="Acyclovir">acyclovir</a>.<a href="#cite_note-65">[65]</a> <div class="mw-heading mw-heading3"><h3 id="Some_examples">Some examples</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=19" title="Edit section: Some examples">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:PDB_1GXF.png" class="mw-file-description"><img alt="3D cartoon diagram of the trypanothione reductase protein bound to two molecules of inhibitors depicted as a stick diagrams." src="//upload.wikimedia.org/wikipedia/commons/thumb/9/9b/PDB_1GXF.png/250px-PDB_1GXF.png" decoding="async" width="220" height="159" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/9b/PDB_1GXF.png/330px-PDB_1GXF.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/9b/PDB_1GXF.png/500px-PDB_1GXF.png 2x" data-file-width="2559" data-file-height="1855" /></a><figcaption><a href="/wiki/Trypanothione" title="Trypanothione">Trypanothione reductase</a> with the lower molecule of an inhibitor bound irreversibly and the upper one reversibly. Created from Bond et al, 2004.<a href="#cite_note-pmid15102853-66">[66]</a> (<a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1GXF">1GXF</a>)</figcaption></figure> <a href="/wiki/Diisopropylfluorophosphate" class="mw-redirect" title="Diisopropylfluorophosphate">Diisopropylfluorophosphate</a> (DFP) is an example of an irreversible <a href="/wiki/Protease_inhibitor_(pharmacology)" title="Protease inhibitor (pharmacology)">protease inhibitor</a> (see the "DFP reaction" diagram). The enzyme hydrolyses the phosphorus–fluorine bond, but the phosphate residue remains bound to the serine in the <a href="/wiki/Catalytic_triad" title="Catalytic triad">active site</a>, deactivating it.<a href="#cite_note-67">[67]</a> Similarly, DFP also reacts with the active site of <a href="/wiki/Acetylcholine_esterase" class="mw-redirect" title="Acetylcholine esterase">acetylcholine esterase</a> in the <a href="/wiki/Synapses" class="mw-redirect" title="Synapses">synapses</a> of neurons, and consequently is a potent neurotoxin, with a lethal dose of less than 100 mg.<a href="#cite_note-68">[68]</a> <a href="/wiki/Suicide_inhibition" title="Suicide inhibition">Suicide inhibition</a> is an unusual type of irreversible inhibition where the enzyme converts the inhibitor into a reactive form in its active site.<a href="#cite_note-Walsh_1984-69">[69]</a> An example is the inhibitor of <a href="/wiki/Polyamine" title="Polyamine">polyamine</a> biosynthesis, <a href="/wiki/Eflornithine" title="Eflornithine">α-difluoromethylornithine</a> (DFMO), which is an analogue of the amino acid <a href="/wiki/Ornithine" title="Ornithine">ornithine</a>, and is used to treat <a href="/wiki/African_trypanosomiasis" title="African trypanosomiasis">African trypanosomiasis</a> (sleeping sickness). <a href="/wiki/Ornithine_decarboxylase" title="Ornithine decarboxylase">Ornithine decarboxylase</a> can catalyse the decarboxylation of DFMO instead of ornithine (see the "DFMO inhibitor mechanism" diagram). However, this decarboxylation reaction is followed by the elimination of a fluorine atom, which converts this catalytic intermediate into a conjugated <a href="/wiki/Imine" title="Imine">imine</a>, a highly electrophilic species. This reactive form of DFMO then reacts with either a cysteine or lysine residue in the active site to irreversibly inactivate the enzyme.<a href="#cite_note-Poulin-61">[61]</a> Since irreversible inhibition often involves the initial formation of a non-covalent enzyme inhibitor (EI) complex,<a href="#cite_note-Tuley_2018-13">[13]</a> it is sometimes possible for an inhibitor to bind to an enzyme in more than one way. For example, in the figure showing <a href="/wiki/Trypanothione" title="Trypanothione">trypanothione reductase</a> from the human protozoan parasite <a href="/wiki/Trypanosoma_cruzi" title="Trypanosoma cruzi">Trypanosoma cruzi</a>, two molecules of an inhibitor called quinacrine mustard are bound in its active site. The top molecule is bound reversibly, but the lower one is bound covalently as it has reacted with an amino acid residue through its <a href="/wiki/Nitrogen_mustard" title="Nitrogen mustard">nitrogen mustard</a> group.<a href="#cite_note-70">[70]</a> <div class="mw-heading mw-heading2"><h2 id="Applications">Applications</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=20" title="Edit section: Applications">edit</a>]</div> Enzyme inhibitors are found in nature<a href="#cite_note-71">[71]</a> and also produced artificially in the laboratory.<a href="#cite_note-Hiratake_2005-72">[72]</a> Naturally occurring enzyme inhibitors regulate many <a href="/wiki/Metabolic" class="mw-redirect" title="Metabolic">metabolic</a> processes and are essential for life.<a href="#cite_note-Plaxton_2004-3">[3]</a><a href="#cite_note-Copeland_2013-1">[1]</a> In addition, naturally produced <a href="/wiki/Poison" title="Poison">poisons</a> are often enzyme inhibitors that have evolved for use as toxic agents against predators, prey, and competing organisms.<a href="#cite_note-Haefner_2003-4">[4]</a> These natural toxins include some of the most poisonous substances known.<a href="#cite_note-73">[73]</a> Artificial inhibitors are often used as drugs, but can also be <a href="/wiki/Insecticide" title="Insecticide">insecticides</a> such as <a href="/wiki/Malathion" title="Malathion">malathion</a>, <a href="/wiki/Herbicide" title="Herbicide">herbicides</a> such as <a href="/wiki/Glyphosate" title="Glyphosate">glyphosate</a>,<a href="#cite_note-74">[74]</a> or <a href="/wiki/Disinfectant" title="Disinfectant">disinfectants</a> such as <a href="/wiki/Triclosan" title="Triclosan">triclosan</a>. Other artificial enzyme inhibitors block <a href="/wiki/Acetylcholinesterase" title="Acetylcholinesterase">acetylcholinesterase</a>, an enzyme which breaks down <a href="/wiki/Acetylcholine" title="Acetylcholine">acetylcholine</a>, and are used as <a href="/wiki/Nerve_agent" title="Nerve agent">nerve agents</a> in <a href="/wiki/Chemical_warfare" title="Chemical warfare">chemical warfare</a>.<a href="#cite_note-75">[75]</a> <div class="mw-heading mw-heading3"><h3 id="Metabolic_regulation">Metabolic regulation</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=21" title="Edit section: Metabolic regulation">edit</a>]</div> Enzyme inhibition is a common feature of <a href="/wiki/Metabolic_pathway" title="Metabolic pathway">metabolic pathway</a> control in cells.<a href="#cite_note-Plaxton_2004-3">[3]</a> <a href="/wiki/Metabolic_flux" class="mw-redirect" title="Metabolic flux">Metabolic flux</a> through a pathway is often regulated by a pathway's <a href="/wiki/Metabolites" class="mw-redirect" title="Metabolites">metabolites</a> acting as inhibitors and enhancers for the enzymes in that same pathway. The <a href="/wiki/Glycolysis" title="Glycolysis">glycolytic pathway</a> is a classic example.<a href="#cite_note-Orencio-Trejo_2010-76">[76]</a> This <a href="/wiki/Catabolism" title="Catabolism">catabolic</a> pathway consumes <a href="/wiki/Glucose" title="Glucose">glucose</a> and produces <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>, <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NADH</a> and <a href="/wiki/Pyruvate" class="mw-redirect" title="Pyruvate">pyruvate</a>. A key step for the regulation of glycolysis is an early reaction in the pathway catalysed by <a href="/wiki/Phosphofructokinase" title="Phosphofructokinase">phosphofructokinase‑1</a> (PFK1). When ATP levels rise, ATP binds an allosteric site in PFK1 to decrease the rate of the enzyme reaction; glycolysis is inhibited and ATP production falls. This <a href="/wiki/Feedback" title="Feedback">negative feedback</a> control helps maintain a steady concentration of ATP in the cell. However, metabolic pathways are not just regulated through inhibition since enzyme activation is equally important. With respect to PFK1, <a href="/wiki/Fructose_2,6-bisphosphate" title="Fructose 2,6-bisphosphate">fructose 2,6-bisphosphate</a> and <a href="/wiki/Adenosine_diphosphate" title="Adenosine diphosphate">ADP</a> are examples of metabolites that are allosteric activators.<a href="#cite_note-77">[77]</a> Physiological enzyme inhibition can also be produced by specific protein inhibitors. This mechanism occurs in the <a href="/wiki/Pancreas" title="Pancreas">pancreas</a>, which synthesises many digestive precursor enzymes known as <a href="/wiki/Zymogen" title="Zymogen">zymogens</a>. Many of these are activated by the <a href="/wiki/Trypsin" title="Trypsin">trypsin</a> protease, so it is important to inhibit the activity of trypsin in the pancreas to prevent the organ from digesting itself. One way in which the activity of trypsin is controlled is the production of a specific and potent <a href="/wiki/Trypsin_inhibitor" title="Trypsin inhibitor">trypsin inhibitor</a> protein in the pancreas. This inhibitor binds tightly to trypsin, preventing the trypsin activity that would otherwise be detrimental to the organ.<a href="#cite_note-78">[78]</a> Although the trypsin inhibitor is a protein, it avoids being hydrolysed as a substrate by the protease by excluding water from trypsin's active site and destabilising the transition state.<a href="#cite_note-79">[79]</a> Other examples of physiological enzyme inhibitor proteins include the <a href="/wiki/Barstar" title="Barstar">barstar</a> inhibitor of the bacterial ribonuclease <a href="/wiki/Barnase" title="Barnase">barnase</a>.<a href="#cite_note-80">[80]</a> <div class="mw-heading mw-heading3"><h3 id="Natural_poisons">Natural poisons</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=22" title="Edit section: Natural poisons">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:3_types_of_lentil.jpg" class="mw-file-description"><img alt="photo of three piles of legume seeds coloured brown, pea green, and brown/orange" src="//upload.wikimedia.org/wikipedia/commons/thumb/d/da/3_types_of_lentil.jpg/220px-3_types_of_lentil.jpg" decoding="async" width="220" height="124" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/da/3_types_of_lentil.jpg/330px-3_types_of_lentil.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/da/3_types_of_lentil.jpg/440px-3_types_of_lentil.jpg 2x" data-file-width="3840" data-file-height="2160" /></a><figcaption>To discourage <a href="/wiki/Seed_predation" title="Seed predation">seed predation</a>, <a href="/wiki/Legume" title="Legume">legumes</a> contain <a href="/wiki/Trypsin_inhibitor" title="Trypsin inhibitor">trypsin inhibitors</a> that interfere with digestion.</figcaption></figure> Animals and plants have evolved to synthesise a vast array of poisonous products including <a href="/wiki/Secondary_metabolite" title="Secondary metabolite">secondary metabolites</a>,<a href="#cite_note-81">[81]</a> peptides and proteins<a href="#cite_note-82">[82]</a> that can act as inhibitors. Natural toxins are usually <a href="/wiki/Small_molecule" title="Small molecule">small organic molecules</a> and are so diverse that there are probably natural inhibitors for most metabolic processes.<a href="#cite_note-83">[83]</a> The metabolic processes targeted by natural poisons encompass more than enzymes in metabolic pathways and can also include the inhibition of receptor, channel and structural protein functions in a cell. For example, <a href="/wiki/Paclitaxel" title="Paclitaxel">paclitaxel</a> (taxol), an organic molecule found in the <a href="/wiki/Taxus" title="Taxus">Pacific yew tree</a>, binds tightly to <a href="/wiki/Tubulin" title="Tubulin">tubulin</a> <a href="/wiki/Protein_dimer" title="Protein dimer">dimers</a> and inhibits their assembly into <a href="/wiki/Microtubule" title="Microtubule">microtubules</a> in the <a href="/wiki/Cytoskeleton" title="Cytoskeleton">cytoskeleton</a>.<a href="#cite_note-84">[84]</a> Many natural poisons act as <a href="/wiki/Neurotoxin" title="Neurotoxin">neurotoxins</a> that can cause <a href="/wiki/Paralysis" title="Paralysis">paralysis</a> leading to death and function for defence against predators or in hunting and capturing prey. Some of these natural inhibitors,<a href="#cite_note-Hostettmann_2006-85">[85]</a> despite their toxic attributes, are valuable for therapeutic uses at lower doses.<a href="#cite_note-Knight_2018-86">[86]</a> An example of a neurotoxin are the <a href="/wiki/Glycoalkaloid" title="Glycoalkaloid">glycoalkaloids</a>, from the plant species in the family <a href="/wiki/Solanaceae" title="Solanaceae">Solanaceae</a> (includes <a href="/wiki/Potato" title="Potato">potato</a>, <a href="/wiki/Tomato" title="Tomato">tomato</a> and <a href="/wiki/Eggplant" title="Eggplant">eggplant</a>), that are <a href="/wiki/Acetylcholinesterase_inhibitor" title="Acetylcholinesterase inhibitor">acetylcholinesterase inhibitors</a>. Inhibition of this enzyme causes an uncontrolled increase in the acetylcholine neurotransmitter, muscular paralysis and then death. <a href="/wiki/Neurotoxicity" title="Neurotoxicity">Neurotoxicity</a> can also result from the inhibition of receptors; for example, <a href="/wiki/Atropine" title="Atropine">atropine</a> from deadly nightshade (<a href="/wiki/Atropa_belladonna" class="mw-redirect" title="Atropa belladonna">Atropa belladonna</a>) that functions as a <a href="/wiki/Competitive_antagonist" class="mw-redirect" title="Competitive antagonist">competitive antagonist</a> of the <a href="/wiki/Acetylcholine_receptor" title="Acetylcholine receptor">muscarinic acetylcholine receptors</a>.<a href="#cite_note-87">[87]</a> Although many natural toxins are secondary metabolites, these poisons also include peptides and proteins. An example of a toxic peptide is <a href="/wiki/Alpha-amanitin" class="mw-redirect" title="Alpha-amanitin">alpha-amanitin</a>, which is found in relatives of the <a href="/wiki/Death_cap" class="mw-redirect" title="Death cap">death cap</a> mushroom. This is a potent enzyme inhibitor, in this case preventing the <a href="/wiki/RNA_polymerase_II" title="RNA polymerase II">RNA polymerase II</a> enzyme from transcribing DNA.<a href="#cite_note-88">[88]</a> The algal toxin <a href="/wiki/Microcystin" title="Microcystin">microcystin</a> is also a peptide and is an inhibitor of <a href="/wiki/Phosphatase" title="Phosphatase">protein phosphatases</a>.<a href="#cite_note-89">[89]</a> This toxin can contaminate water supplies after <a href="/wiki/Algal_bloom" title="Algal bloom">algal blooms</a> and is a known carcinogen that can also cause acute liver haemorrhage and death at higher doses.<a href="#cite_note-90">[90]</a> Proteins can also be natural poisons or <a href="/wiki/Antinutrient" title="Antinutrient">antinutrients</a>, such as the <a href="/wiki/Trypsin_inhibitor" title="Trypsin inhibitor">trypsin inhibitors</a> (discussed in the "metabolic regulation" section above) that are found in some <a href="/wiki/Pulse_(legume)" class="mw-redirect" title="Pulse (legume)">legumes</a>.<a href="#cite_note-91">[91]</a> A less common class of toxins are toxic enzymes: these act as irreversible inhibitors of their target enzymes and work by chemically modifying their substrate enzymes. An example is <a href="/wiki/Ricin" title="Ricin">ricin</a>, an extremely potent protein toxin found in <a href="/wiki/Castor_oil_plant" class="mw-redirect" title="Castor oil plant">castor oil beans</a>.<a href="#cite_note-Polito_2019-92">[92]</a> This enzyme is a <a href="/wiki/Glycosidase" class="mw-redirect" title="Glycosidase">glycosidase</a> that inactivates ribosomes.<a href="#cite_note-Sowa-Rogozińska_2019-93">[93]</a> Since ricin is a catalytic irreversible inhibitor, this allows just a single molecule of ricin to kill a cell.<a href="#cite_note-94">[94]</a> <div class="mw-heading mw-heading3"><h3 id="Drugs">Drugs</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=23" title="Edit section: Drugs">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Methotrexate_vs_folate.svg" class="mw-file-description"><img alt="2D chemical structural diagrams comparing folic acid and methotrexate" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Methotrexate_vs_folate.svg/220px-Methotrexate_vs_folate.svg.png" decoding="async" width="220" height="146" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Methotrexate_vs_folate.svg/330px-Methotrexate_vs_folate.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/21/Methotrexate_vs_folate.svg/440px-Methotrexate_vs_folate.svg.png 2x" data-file-width="616" data-file-height="409" /></a><figcaption>The coenzyme folic acid (top) compared to the anti-cancer drug methotrexate (bottom)</figcaption></figure> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Sildenafil.svg" class="mw-file-description"><img alt="2D structural diagram of sildenafil" src="//upload.wikimedia.org/wikipedia/commons/thumb/4/48/Sildenafil.svg/220px-Sildenafil.svg.png" decoding="async" width="220" height="115" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/48/Sildenafil.svg/330px-Sildenafil.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/48/Sildenafil.svg/440px-Sildenafil.svg.png 2x" data-file-width="512" data-file-height="268" /></a><figcaption>The structure of <a href="/wiki/Sildenafil" title="Sildenafil">sildenafil</a> (Viagra)</figcaption></figure> The most common uses for enzyme inhibitors are as drugs to treat disease. Many of these inhibitors target a human enzyme and aim to correct a pathological condition. For instance, <a href="/wiki/Aspirin" title="Aspirin">aspirin</a> is a widely used drug that acts as a <a href="/wiki/Suicide_inhibitor" class="mw-redirect" title="Suicide inhibitor">suicide inhibitor</a> of the <a href="/wiki/Cyclooxygenase" title="Cyclooxygenase">cyclooxygenase</a> enzyme.<a href="#cite_note-Finkel_2009-95">[95]</a> This inhibition in turn suppresses the production of proinflammatory <a href="/wiki/Prostaglandin" title="Prostaglandin">prostaglandins</a> and thus aspirin may be used to reduce pain, fever, and inflammation.<a href="#cite_note-Finkel_2009-95">[95]</a> As of 2017,<a class="external text" href="https://en.wikipedia.org/w/index.php?title=Enzyme_inhibitor&action=edit">[update]</a> an estimated 29% of approved drugs are enzyme inhibitors<a href="#cite_note-Santos_2017-96">[96]</a> of which approximately one-fifth are <a href="/wiki/Kinase" title="Kinase">kinase</a> inhibitors.<a href="#cite_note-Santos_2017-96">[96]</a> A notable class of kinase drug targets is the <a href="/wiki/Receptor_tyrosine_kinase" title="Receptor tyrosine kinase">receptor tyrosine kinases</a> which are essential enzymes that regulate <a href="/wiki/Cell_growth" title="Cell growth">cell growth</a>; their over-activation may result in cancer. Hence <a href="/wiki/Kinase_inhibitor" class="mw-redirect" title="Kinase inhibitor">kinase inhibitors</a> such as <a href="/wiki/Imatinib" title="Imatinib">imatinib</a> are frequently used to treat malignancies.<a href="#cite_note-Kannaiyan_2018-97">[97]</a> <a href="/wiki/Janus_kinase" title="Janus kinase">Janus kinases</a> are another notable example of drug enzyme targets. <a href="/wiki/Janus_kinase_inhibitor" title="Janus kinase inhibitor">Inhibitors of Janus kinases</a> block the production of <a href="/wiki/Inflammatory_cytokine" title="Inflammatory cytokine">inflammatory cytokines</a> and hence these inhibitors are used to treat a variety of <a href="/wiki/Inflammatory_disease" class="mw-redirect" title="Inflammatory disease">inflammatory diseases</a> in including <a href="/wiki/Arthritis" title="Arthritis">arthritis</a>, <a href="/wiki/Asthma" title="Asthma">asthma</a>, and <a href="/wiki/Crohn%27s_disease" title="Crohn's disease">Crohn's disease</a>.<a href="#cite_note-McLornan_2021-98">[98]</a> An example of the structural similarity of some inhibitors to the substrates of the enzymes they target is seen in the figure comparing the drug <a href="/wiki/Methotrexate" title="Methotrexate">methotrexate</a> to <a href="/wiki/Folic_acid" class="mw-redirect" title="Folic acid">folic acid</a>. Folic acid is the oxidised form of the substrate of <a href="/wiki/Dihydrofolate_reductase" title="Dihydrofolate reductase">dihydrofolate reductase</a>, an enzyme that is potently inhibited by methotrexate. Methotrexate blocks the action of dihydrofolate reductase and thereby halts <a href="/wiki/Thymidine" title="Thymidine">thymidine</a> biosynthesis.<a href="#cite_note-Avendano_2015-42">[42]</a> This block of <a href="/wiki/Nucleotide" title="Nucleotide">nucleotide</a> biosynthesis is selectively toxic to rapidly growing cells, therefore methotrexate is often used in cancer chemotherapy.<a href="#cite_note-99">[99]</a> A common treatment for <a href="/wiki/Erectile_dysfunction" title="Erectile dysfunction">erectile dysfunction</a> is <a href="/wiki/Sildenafil" title="Sildenafil">sildenafil</a> (Viagra).<a href="#cite_note-common_2019-100">[100]</a> This compound is a potent inhibitor of <a href="/wiki/CGMP_specific_phosphodiesterase_type_5" class="mw-redirect" title="CGMP specific phosphodiesterase type 5">cGMP specific phosphodiesterase type 5</a>, the enzyme that degrades the signalling molecule <a href="/wiki/Cyclic_guanosine_monophosphate" title="Cyclic guanosine monophosphate">cyclic guanosine monophosphate</a>.<a href="#cite_note-101">[101]</a> This signalling molecule triggers smooth muscle relaxation and allows blood flow into the <a href="/wiki/Corpus_cavernosum_penis" title="Corpus cavernosum penis">corpus cavernosum</a>, which causes an erection. Since the drug decreases the activity of the enzyme that halts the signal, it makes this signal last for a longer period of time. <div class="mw-heading mw-heading4"><h4 id="Antibiotics">Antibiotics</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=24" title="Edit section: Antibiotics">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:PDB_1PWC.png" class="mw-file-description"><img alt="3D cartoon diagram of transpeptidase bound to penicillin G depicted as sticks" src="//upload.wikimedia.org/wikipedia/commons/thumb/1/18/PDB_1PWC.png/220px-PDB_1PWC.png" decoding="async" width="220" height="159" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/18/PDB_1PWC.png/330px-PDB_1PWC.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/18/PDB_1PWC.png/440px-PDB_1PWC.png 2x" data-file-width="2559" data-file-height="1855" /></a><figcaption>The structure of a complex between penicillin G and the Streptomyces transpeptidase (<a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1PWC">1PWC</a>)</figcaption></figure> Drugs are also used to inhibit enzymes needed for the survival of pathogens. For example, bacteria are surrounded by a thick <a href="/wiki/Bacterial_cell_structure" title="Bacterial cell structure">cell wall</a> made of a net-like polymer called <a href="/wiki/Peptidoglycan" title="Peptidoglycan">peptidoglycan</a>. Many <a href="/wiki/Antibiotic" title="Antibiotic">antibiotics</a> such as <a href="/wiki/Penicillin" title="Penicillin">penicillin</a> and <a href="/wiki/Vancomycin" title="Vancomycin">vancomycin</a> inhibit the enzymes that produce and then cross-link the strands of this polymer together.<a href="#cite_note-Cochrane_2020-102">[102]</a><a href="#cite_note-Buynak_2007-103">[103]</a> This causes the cell wall to lose strength and the bacteria to burst. In the figure, a molecule of penicillin (shown in a ball-and-stick form) is shown bound to its target, the <a href="/wiki/DD-Transpeptidase" title="DD-Transpeptidase">transpeptidase</a> from the bacteria Streptomyces R61 (the protein is shown as a <a href="/wiki/Ribbon_diagram" title="Ribbon diagram">ribbon diagram</a>). Antibiotic <a href="/wiki/Drug_design" title="Drug design">drug design</a> is facilitated when an enzyme that is essential to the pathogen's survival is absent or very different in humans.<a href="#cite_note-Dalhoff_2021-104">[104]</a> Humans do not make peptidoglycan, therefore antibiotics that inhibit this process are selectively toxic to bacteria.<a href="#cite_note-105">[105]</a> Selective toxicity is also produced in antibiotics by exploiting differences in the structure of the <a href="/wiki/Ribosome" title="Ribosome">ribosomes</a> in bacteria,<a href="#cite_note-Zhang_2021-106">[106]</a> or how they make <a href="/wiki/Fatty_acid" title="Fatty acid">fatty acids</a>.<a href="#cite_note-Yao_2017-107">[107]</a> <div class="mw-heading mw-heading4"><h4 id="Antivirals">Antivirals</h4>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=25" title="Edit section: Antivirals">edit</a>]</div> Drugs that inhibit enzymes needed for the <a href="/wiki/Viral_replication" title="Viral replication">replication of viruses</a> are effective in treating viral infections.<a href="#cite_note-108">[108]</a> <a href="/wiki/Antiviral_drug" title="Antiviral drug">Antiviral drugs</a> include <a href="/wiki/Protease_inhibitors" class="mw-redirect" title="Protease inhibitors">protease inhibitors</a> used to treat <a href="/wiki/HIV/AIDS" title="HIV/AIDS">HIV/AIDS</a><a href="#cite_note-Voshavar_2019-109">[109]</a> and <a href="/wiki/Hepatitis_C" title="Hepatitis C">Hepatitis C</a>,<a href="#cite_note-de_Leuw_2018-110">[110]</a> <a href="/wiki/Reverse-transcriptase_inhibitor" title="Reverse-transcriptase inhibitor">reverse-transcriptase inhibitors</a> targeting HIV/AIDS,<a href="#cite_note-Li_2011-111">[111]</a> <a href="/wiki/Neuraminidase_inhibitor" title="Neuraminidase inhibitor">neuraminidase inhibitors</a> targeting <a href="/wiki/Influenza" title="Influenza">influenza</a>,<a href="#cite_note-Gubareva_2022-112">[112]</a> and terminase inhibitors targeting <a href="/wiki/Human_cytomegalovirus" title="Human cytomegalovirus">human cytomegalovirus</a>.<a href="#cite_note-Gentry_2019-113">[113]</a> <div class="mw-heading mw-heading3"><h3 id="Pesticides">Pesticides</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=26" title="Edit section: Pesticides">edit</a>]</div> Many <a href="/wiki/Pesticide" title="Pesticide">pesticides</a> are enzyme inhibitors.<a href="#cite_note-114">[114]</a> <a href="/wiki/Acetylcholinesterase" title="Acetylcholinesterase">Acetylcholinesterase</a> (AChE) is an enzyme found in animals, from insects to humans. It is essential to nerve cell function through its mechanism of breaking down the neurotransmitter <a href="/wiki/Acetylcholine" title="Acetylcholine">acetylcholine</a> into its constituents, <a href="/wiki/Acetate" title="Acetate">acetate</a> and <a href="/wiki/Choline" title="Choline">choline</a>.<a href="#cite_note-115">[115]</a> This is somewhat unusual among neurotransmitters as most, including <a href="/wiki/Serotonin" title="Serotonin">serotonin</a>, <a href="/wiki/Dopamine" title="Dopamine">dopamine</a>, and <a href="/wiki/Norepinephrine" title="Norepinephrine">norepinephrine</a>, are absorbed from the <a href="/wiki/Synaptic_cleft" class="mw-redirect" title="Synaptic cleft">synaptic cleft</a> rather than cleaved. A large number of AChE inhibitors are used in both medicine and agriculture.<a href="#cite_note-Gupta_2006-116">[116]</a> Reversible competitive inhibitors, such as <a href="/wiki/Edrophonium" title="Edrophonium">edrophonium</a>, <a href="/wiki/Physostigmine" title="Physostigmine">physostigmine</a>, and <a href="/wiki/Neostigmine" title="Neostigmine">neostigmine</a>, are used in the treatment of <a href="/wiki/Myasthenia_gravis" title="Myasthenia gravis">myasthenia gravis</a><a href="#cite_note-Farmakidis_2018-117">[117]</a> and in anaesthesia to reverse muscle blockade.<a href="#cite_note-118">[118]</a> The <a href="/wiki/Carbamate" title="Carbamate">carbamate</a> pesticides are also examples of reversible AChE inhibitors. The <a href="/wiki/Organophosphate" title="Organophosphate">organophosphate</a> pesticides such as <a href="/wiki/Malathion" title="Malathion">malathion</a>, <a href="/wiki/Parathion" title="Parathion">parathion</a>, and <a href="/wiki/Chlorpyrifos" title="Chlorpyrifos">chlorpyrifos</a> irreversibly inhibit acetylcholinesterase.<a href="#cite_note-Thapa_2017-119">[119]</a> <div class="mw-heading mw-heading3"><h3 id="Herbicides">Herbicides</h3>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=27" title="Edit section: Herbicides">edit</a>]</div> The herbicide <a href="/wiki/Glyphosate" title="Glyphosate">glyphosate</a> is an inhibitor of <a href="/wiki/3-phosphoshikimate_1-carboxyvinyltransferase" class="mw-redirect" title="3-phosphoshikimate 1-carboxyvinyltransferase">3-phosphoshikimate 1-carboxyvinyltransferase</a>,<a href="#cite_note-pmid16547651-120">[120]</a> other herbicides, such as the <a href="/wiki/Sulfonylurea" title="Sulfonylurea">sulfonylureas</a> inhibit the enzyme <a href="/wiki/Acetolactate_synthase" title="Acetolactate synthase">acetolactate synthase</a>.<a href="#cite_note-121">[121]</a> Both enzymes are needed for plants to make branched-chain <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a>. Many other enzymes are inhibited by herbicides, including enzymes needed for the biosynthesis of <a href="/wiki/Lipid" title="Lipid">lipids</a> and <a href="/wiki/Carotenoid" title="Carotenoid">carotenoids</a> and the processes of <a href="/wiki/Photosynthesis" title="Photosynthesis">photosynthesis</a> and <a href="/wiki/Oxidative_phosphorylation" title="Oxidative phosphorylation">oxidative phosphorylation</a>.<a href="#cite_note-122">[122]</a> <div class="mw-heading mw-heading2"><h2 id="Discovery_and_design">Discovery and design</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=28" title="Edit section: Discovery and design">edit</a>]</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Screening_robotics_for_HTS-1-.jpg" class="mw-file-description"><img alt="photo of robots at work" src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a8/Screening_robotics_for_HTS-1-.jpg/220px-Screening_robotics_for_HTS-1-.jpg" decoding="async" width="220" height="147" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/a/a8/Screening_robotics_for_HTS-1-.jpg 1.5x" data-file-width="315" data-file-height="211" /></a><figcaption>Robots are used for the high-throughput screening of chemical libraries to discover new enzyme inhibitors.</figcaption></figure> New drugs are the products of a long <a href="/wiki/Drug_development" title="Drug development">drug development</a> process, the first step of which is often the discovery of a new enzyme inhibitor.<a href="#cite_note-123">[123]</a> There are two principle approaches of discovering these inhibitors.<a href="#cite_note-Rufer_2021-124">[124]</a> The first general method is <a href="/wiki/Rational_drug_design" class="mw-redirect" title="Rational drug design">rational drug design</a> based on mimicking the <a href="/wiki/Transition_state" title="Transition state">transition state</a> of the chemical reaction catalysed by the enzyme.<a href="#cite_note-125">[125]</a> The designed inhibitor often closely resembles the substrate, except that the portion of the substrate that undergoes chemical reaction is replaced by a chemically stable <a href="/wiki/Functional_group" title="Functional group">functional group</a> that resembles the transition state. Since the enzyme has evolved to stabilise the transition state, <a href="/wiki/Transition_state_analogue" class="mw-redirect" title="Transition state analogue">transition state analogues</a> generally possess higher affinity for the enzyme compared to the substrate, and therefore are effective inhibitors.<a href="#cite_note-Schramm_2018-46">[46]</a> The second way of discovering new enzyme inhibitors is <a href="/wiki/High-throughput_screening" title="High-throughput screening">high-throughput screening</a> of large libraries of structurally diverse compounds to identify hit molecules that bind to the enzyme. This method has been extended to include <a href="/wiki/Virtual_screening" title="Virtual screening">virtual screening</a> of databases of diverse molecules using computers,<a href="#cite_note-126">[126]</a><a href="#cite_note-127">[127]</a> which are then followed by experimental confirmation of binding of the virtual screening hits.<a href="#cite_note-128">[128]</a> Complementary approaches that can provide new starting points for inhibitors include <a href="/wiki/Fragment-based_lead_discovery" title="Fragment-based lead discovery">fragment-based lead discovery</a><a href="#cite_note-Ciulli_2007-129">[129]</a> and <a href="/wiki/DNA_Encoded_Chemical_Libraries" class="mw-redirect" title="DNA Encoded Chemical Libraries">DNA Encoded Chemical Libraries</a> (DEL).<a href="#cite_note-Satz_2021-130">[130]</a> Hits from any of the above approaches can be <a href="/wiki/Hit_to_lead" title="Hit to lead">optimised</a> to high affinity binders that efficiently inhibit the enzyme.<a href="#cite_note-131">[131]</a> <a href="/wiki/Drug_design" title="Drug design">Computer-based methods</a> for predicting the binding orientation and affinity of an inhibitor for an enzyme such as <a href="/wiki/Molecular_docking" class="mw-redirect" title="Molecular docking">molecular docking</a><a href="#cite_note-Scarpino_2020-132">[132]</a> and <a href="/wiki/Molecular_mechanics" title="Molecular mechanics">molecular mechanics</a> can be used to assist in the optimisation process.<a href="#cite_note-133">[133]</a> New inhibitors are used to obtain <a href="/wiki/X-ray_crystallography#Biological_macromolecular_crystallography" title="X-ray crystallography">crystallographic structures</a> of the enzyme in an inhibitor/enzyme complex to show how the molecule is binding to the active site, allowing changes to be made to the inhibitor to optimise binding in a process known as <a href="/wiki/Drug_design#Structure-based" title="Drug design">structure-based drug design</a>.<a href="#cite_note-Copeland_2013-1">[1]</a>: 66  This test and improve cycle is repeated until a sufficiently potent inhibitor is produced. <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=29" title="Edit section: See also">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1266661725">.mw-parser-output .portalbox{padding:0;margin:0.5em 0;display:table;box-sizing:border-box;max-width:175px;list-style:none}.mw-parser-output .portalborder{border:1px solid var(--border-color-base,#a2a9b1);padding:0.1em;background:var(--background-color-neutral-subtle,#f8f9fa)}.mw-parser-output .portalbox-entry{display:table-row;font-size:85%;line-height:110%;height:1.9em;font-style:italic;font-weight:bold}.mw-parser-output .portalbox-image{display:table-cell;padding:0.2em;vertical-align:middle;text-align:center}.mw-parser-output .portalbox-link{display:table-cell;padding:0.2em 0.2em 0.2em 0.3em;vertical-align:middle}@media(min-width:720px){.mw-parser-output .portalleft{margin:0.5em 1em 0.5em 0}.mw-parser-output .portalright{clear:right;float:right;margin:0.5em 0 0.5em 1em}}</style><ul role="navigation" aria-label="Portals" class="noprint portalbox portalborder portalright"> <li class="portalbox-entry"><a href="/wiki/File:Issoria_lathonia.jpg" class="mw-file-description"><img alt="icon" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/32px-Issoria_lathonia.jpg" decoding="async" width="32" height="23" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/48px-Issoria_lathonia.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/64px-Issoria_lathonia.jpg 2x" data-file-width="629" data-file-height="445" /></a><a href="/wiki/Portal:Biology" title="Portal:Biology">Biology portal</a></li></ul> <ul><li><a href="/wiki/Activity-based_proteomics" title="Activity-based proteomics">Activity-based proteomics</a> – a branch of <a href="/wiki/Proteomics" title="Proteomics">proteomics</a> that uses covalent enzyme inhibitors as reporters to monitor enzyme activity.</li> <li><a href="/wiki/Antimetabolite" title="Antimetabolite">Antimetabolite</a> – an enzyme inhibitor that is used to interfere with cell growth and division</li> <li><a href="/wiki/Transition_state_analogue" class="mw-redirect" title="Transition state analogue">Transition state analogue</a> – a type of enzyme inhibitor that mimics the transition state of the chemical reaction catalysed by the enzyme</li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=30" title="Edit section: References">edit</a>]</div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-Copeland_2013-1">^ <a href="#cite_ref-Copeland_2013_1-0">a</a> <a href="#cite_ref-Copeland_2013_1-1">b</a> <a href="#cite_ref-Copeland_2013_1-2">c</a> <a href="#cite_ref-Copeland_2013_1-3">d</a> <style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFCopeland2013" class="citation book cs1">Copeland RA (March 2013). "Why Enzymes as Drug Targets? Enzyme are Essential for Life". Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (Second ed.). John Wiley & Sons, Inc. pp. 1–23. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2F9781118540398.ch1">10.1002/9781118540398.ch1</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-118-48813-3" title="Special:BookSources/978-1-118-48813-3"><bdi>978-1-118-48813-3</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Why+Enzymes+as+Drug+Targets%3F+Enzyme+are+Essential+for+Life&rft.btitle=Evaluation+of+Enzyme+Inhibitors+in+Drug+Discovery%3A+A+Guide+for+Medicinal+Chemists+and+Pharmacologists&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1-%3C%2Fspan%3E23&rft.edition=Second&rft.pub=John+Wiley+%26+Sons%2C+Inc.&rft.date=2013-03&rft_id=info%3Adoi%2F10.1002%2F9781118540398.ch1&rft.isbn=978-1-118-48813-3&rft.aulast=Copeland&rft.aufirst=RA&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Sauro_2017-2">^ <a href="#cite_ref-Sauro_2017_2-0">a</a> <a href="#cite_ref-Sauro_2017_2-1">b</a> <a href="#cite_ref-Sauro_2017_2-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSauro2017" class="citation journal cs1">Sauro HM (February 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5332569">"Control and regulation of pathways via negative feedback"</a>. Journal of the Royal Society, Interface. 14 (127): 1–13. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1098%2Frsif.2016.0848">10.1098/rsif.2016.0848</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5332569">5332569</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28202588">28202588</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+the+Royal+Society%2C+Interface&rft.atitle=Control+and+regulation+of+pathways+via+negative+feedback&rft.volume=14&rft.issue=127&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1-%3C%2Fspan%3E13&rft.date=2017-02&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5332569%23id-name%3DPMC&rft_id=info%3Apmid%2F28202588&rft_id=info%3Adoi%2F10.1098%2Frsif.2016.0848&rft.aulast=Sauro&rft.aufirst=HM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5332569&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Plaxton_2004-3">^ <a href="#cite_ref-Plaxton_2004_3-0">a</a> <a href="#cite_ref-Plaxton_2004_3-1">b</a> <a href="#cite_ref-Plaxton_2004_3-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPlaxton2004" class="citation book cs1">Plaxton WC (2004). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=d1nu4vcml8sC&q=inhibitor&pg=PA11">"Principles of Metabolic Control"</a>. In Storey KB (ed.). Functional Metabolism: Regulation and Adaptation. Hoboken, N.J.: John Wiley & Sons. pp. 1–24 (12). <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-471-67557-0" title="Special:BookSources/978-0-471-67557-0"><bdi>978-0-471-67557-0</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328010003/https://books.google.com/books?id=d1nu4vcml8sC&q=inhibitor&pg=PA11">Archived</a> from the original on 28 March 2023. Retrieved 14 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Principles+of+Metabolic+Control&rft.btitle=Functional+Metabolism%3A+Regulation+and+Adaptation&rft.place=Hoboken%2C+N.J.&rft.pages=1-24+%2812%29&rft.pub=John+Wiley+%26+Sons&rft.date=2004&rft.isbn=978-0-471-67557-0&rft.aulast=Plaxton&rft.aufirst=WC&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3Dd1nu4vcml8sC%26q%3Dinhibitor%26pg%3DPA11&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Haefner_2003-4">^ <a href="#cite_ref-Haefner_2003_4-0">a</a> <a href="#cite_ref-Haefner_2003_4-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHaefner2003" class="citation journal cs1">Haefner B (June 2003). "Drugs from the deep: marine natural products as drug candidates". Drug Discovery Today. 8 (12): 536–44. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs1359-6446%2803%2902713-2">10.1016/s1359-6446(03)02713-2</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12821301">12821301</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Drug+Discovery+Today&rft.atitle=Drugs+from+the+deep%3A+marine+natural+products+as+drug+candidates&rft.volume=8&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E536-%3C%2Fspan%3E44&rft.date=2003-06&rft_id=info%3Adoi%2F10.1016%2Fs1359-6446%2803%2902713-2&rft_id=info%3Apmid%2F12821301&rft.aulast=Haefner&rft.aufirst=B&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Gualerzi_2013-5"><a href="#cite_ref-Gualerzi_2013_5-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGualerziBrandiFabbrettiPon2013" class="citation book cs1">Gualerzi CO, Brandi L, Fabbretti A, Pon CL (2013). Antibiotics: Targets, Mechanisms and Resistance. Hoboken: John Wiley & Sons. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-527-65970-8" title="Special:BookSources/978-3-527-65970-8"><bdi>978-3-527-65970-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Antibiotics%3A+Targets%2C+Mechanisms+and+Resistance.&rft.place=Hoboken&rft.pub=John+Wiley+%26+Sons&rft.date=2013&rft.isbn=978-3-527-65970-8&rft.aulast=Gualerzi&rft.aufirst=CO&rft.au=Brandi%2C+L&rft.au=Fabbretti%2C+A&rft.au=Pon%2C+CL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Sanrattana_2019-6"><a href="#cite_ref-Sanrattana_2019_6-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSanrattanaMaasde_Maat2019" class="citation journal cs1">Sanrattana W, Maas C, de Maat S (2019). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6379291">"SERPINs-From Trap to Treatment"</a>. Frontiers in Medicine. 6: 25. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3389%2Ffmed.2019.00025">10.3389/fmed.2019.00025</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6379291">6379291</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30809526">30809526</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Frontiers+in+Medicine&rft.atitle=SERPINs-From+Trap+to+Treatment&rft.volume=6&rft.pages=25&rft.date=2019&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6379291%23id-name%3DPMC&rft_id=info%3Apmid%2F30809526&rft_id=info%3Adoi%2F10.3389%2Ffmed.2019.00025&rft.aulast=Sanrattana&rft.aufirst=W&rft.au=Maas%2C+C&rft.au=de+Maat%2C+S&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6379291&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-7"><a href="#cite_ref-7">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFShapiroVallee1991" class="citation journal cs1">Shapiro R, Vallee BL (February 1991). "Interaction of human placental ribonuclease with placental ribonuclease inhibitor". Biochemistry. 30 (8): 2246–2255. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi00222a030">10.1021/bi00222a030</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/1998683">1998683</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochemistry&rft.atitle=Interaction+of+human+placental+ribonuclease+with+placental+ribonuclease+inhibitor&rft.volume=30&rft.issue=8&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2246-%3C%2Fspan%3E2255&rft.date=1991-02&rft_id=info%3Adoi%2F10.1021%2Fbi00222a030&rft_id=info%3Apmid%2F1998683&rft.aulast=Shapiro&rft.aufirst=R&rft.au=Vallee%2C+BL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Boon_2020-8"><a href="#cite_ref-Boon_2020_8-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBoonUgarte-BerzalVandoorenOpdenakker2020" class="citation journal cs1">Boon L, Ugarte-Berzal E, Vandooren J, Opdenakker G (April 2020). "Protease propeptide structures, mechanisms of activation, and functions". Critical Reviews in Biochemistry and Molecular Biology. 55 (2): 111–165. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F10409238.2020.1742090">10.1080/10409238.2020.1742090</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/32290726">32290726</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:215772580">215772580</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Critical+Reviews+in+Biochemistry+and+Molecular+Biology&rft.atitle=Protease+propeptide+structures%2C+mechanisms+of+activation%2C+and+functions&rft.volume=55&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E111-%3C%2Fspan%3E165&rft.date=2020-04&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A215772580%23id-name%3DS2CID&rft_id=info%3Apmid%2F32290726&rft_id=info%3Adoi%2F10.1080%2F10409238.2020.1742090&rft.aulast=Boon&rft.aufirst=L&rft.au=Ugarte-Berzal%2C+E&rft.au=Vandooren%2C+J&rft.au=Opdenakker%2C+G&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Rydzewski_2010-9">^ <a href="#cite_ref-Rydzewski_2010_9-0">a</a> <a href="#cite_ref-Rydzewski_2010_9-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRydzewski2010" class="citation book cs1">Rydzewski RM (2010). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=9ELvBMCyKKwC&pg=PA288">"Chapter 7.2.1: Competition and Allostery"</a>. Real World Drug Discovery: A Chemist's Guide to Biotech and Pharmaceutical Research (1st ed.). Amsterdam: Elsevier. pp. 281–285. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-08-091488-6" title="Special:BookSources/978-0-08-091488-6"><bdi>978-0-08-091488-6</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328005931/https://books.google.com/books?id=9ELvBMCyKKwC&pg=PA288">Archived</a> from the original on 28 March 2023. Retrieved 20 July 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+7.2.1%3A+Competition+and+Allostery&rft.btitle=Real+World+Drug+Discovery%3A+A+Chemist%27s+Guide+to+Biotech+and+Pharmaceutical+Research&rft.place=Amsterdam&rft.pages=%3Cspan+class%3D%22nowrap%22%3E281-%3C%2Fspan%3E285&rft.edition=1st&rft.pub=Elsevier&rft.date=2010&rft.isbn=978-0-08-091488-6&rft.aulast=Rydzewski&rft.aufirst=RM&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3D9ELvBMCyKKwC%26pg%3DPA288&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-pmid30917186-10"><a href="#cite_ref-pmid30917186_10-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFJakubíkRandákováEl-FakahanyDoležal2019" class="citation journal cs1">Jakubík J, Randáková A, El-Fakahany EE, Doležal V (2019). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6436737">"Analysis of equilibrium binding of an orthosteric tracer and two allosteric modulators"</a>. PLOS ONE. 14 (3): e0214255. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2019PLoSO..1414255J">2019PLoSO..1414255J</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1371%2Fjournal.pone.0214255">10.1371/journal.pone.0214255</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6436737">6436737</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30917186">30917186</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=PLOS+ONE&rft.atitle=Analysis+of+equilibrium+binding+of+an+orthosteric+tracer+and+two+allosteric+modulators&rft.volume=14&rft.issue=3&rft.pages=e0214255&rft.date=2019&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6436737%23id-name%3DPMC&rft_id=info%3Apmid%2F30917186&rft_id=info%3Adoi%2F10.1371%2Fjournal.pone.0214255&rft_id=info%3Abibcode%2F2019PLoSO..1414255J&rft.aulast=Jakub%C3%ADk&rft.aufirst=J&rft.au=Rand%C3%A1kov%C3%A1%2C+A&rft.au=El-Fakahany%2C+EE&rft.au=Dole%C5%BEal%2C+V&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6436737&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Patrick_2013-11"><a href="#cite_ref-Patrick_2013_11-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPatrick2013" class="citation book cs1">Patrick GL (2013). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=Pj7xJRuhZxUC&dq=mechanism+of+allosteric+inhibition+enzyme+catalysis+competitive+noncompetitive&pg=PA90">"Chapter 7: Enzymes as Drug Targets"</a>. An Introduction to Medicinal Chemistry (Fifth ed.). Oxford, UK: Oxford University Press. p. 90. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-19-969739-7" title="Special:BookSources/978-0-19-969739-7"><bdi>978-0-19-969739-7</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220720171418/https://books.google.com/books?id=Pj7xJRuhZxUC&dq=mechanism+of+allosteric+inhibition+enzyme+catalysis+competitive+noncompetitive&pg=PA90">Archived</a> from the original on 20 July 2022. Retrieved 20 July 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+7%3A+Enzymes+as+Drug+Targets&rft.btitle=An+Introduction+to+Medicinal+Chemistry&rft.place=Oxford%2C+UK&rft.pages=90&rft.edition=Fifth&rft.pub=Oxford+University+Press&rft.date=2013&rft.isbn=978-0-19-969739-7&rft.aulast=Patrick&rft.aufirst=GL&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DPj7xJRuhZxUC%26dq%3Dmechanism%2Bof%2Ballosteric%2Binhibition%2Benzyme%2Bcatalysis%2Bcompetitive%2Bnoncompetitive%26pg%3DPA90&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-12"><a href="#cite_ref-12">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKuriyanKonfortiWemmer2012" class="citation book cs1">Kuriyan J, Konforti B, Wemmer D (2012). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=jwcPBAAAQBAJ&pg=PA531">"Molecular Recognition: The Thermodynamics of Binding"</a>. The Molecules of Life : Physical and Chemical Principles (First ed.). Boca Raton, FL: Garland Science. pp. 531–580. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-135-08892-7" title="Special:BookSources/978-1-135-08892-7"><bdi>978-1-135-08892-7</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220607154842/https://books.google.com/books?id=jwcPBAAAQBAJ&pg=PA531">Archived</a> from the original on 7 June 2022. Retrieved 7 June 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Molecular+Recognition%3A+The+Thermodynamics+of+Binding&rft.btitle=The+Molecules+of+Life+%3A+Physical+and+Chemical+Principles&rft.place=Boca+Raton%2C+FL&rft.pages=%3Cspan+class%3D%22nowrap%22%3E531-%3C%2Fspan%3E580&rft.edition=First&rft.pub=Garland+Science&rft.date=2012&rft.isbn=978-1-135-08892-7&rft.aulast=Kuriyan&rft.aufirst=J&rft.au=Konforti%2C+B&rft.au=Wemmer%2C+D&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DjwcPBAAAQBAJ%26pg%3DPA531&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Tuley_2018-13">^ <a href="#cite_ref-Tuley_2018_13-0">a</a> <a href="#cite_ref-Tuley_2018_13-1">b</a> <a href="#cite_ref-Tuley_2018_13-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTuleyFast2018" class="citation journal cs1">Tuley A, Fast W (June 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6016374">"The Taxonomy of Covalent Inhibitors"</a>. Biochemistry. 57 (24): 3326–3337. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Facs.biochem.8b00315">10.1021/acs.biochem.8b00315</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6016374">6016374</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29689165">29689165</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochemistry&rft.atitle=The+Taxonomy+of+Covalent+Inhibitors&rft.volume=57&rft.issue=24&rft.pages=%3Cspan+class%3D%22nowrap%22%3E3326-%3C%2Fspan%3E3337&rft.date=2018-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6016374%23id-name%3DPMC&rft_id=info%3Apmid%2F29689165&rft_id=info%3Adoi%2F10.1021%2Facs.biochem.8b00315&rft.aulast=Tuley&rft.aufirst=A&rft.au=Fast%2C+W&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6016374&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Cleland_1963-14">^ <a href="#cite_ref-Cleland_1963_14-0">a</a> <a href="#cite_ref-Cleland_1963_14-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCleland1963" class="citation journal cs1">Cleland WW (February 1963). "The kinetics of enzyme-catalysed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 67: 173–187. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0926-6569%2863%2990226-8">10.1016/0926-6569(63)90226-8</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14021668">14021668</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Specialized+Section+on+Enzymological+Subjects&rft.atitle=The+kinetics+of+enzyme-catalysed+reactions+with+two+or+more+substrates+or+products.+II.+Inhibition%3A+nomenclature+and+theory&rft.volume=67&rft.pages=%3Cspan+class%3D%22nowrap%22%3E173-%3C%2Fspan%3E187&rft.date=1963-02&rft_id=info%3Adoi%2F10.1016%2F0926-6569%2863%2990226-8&rft_id=info%3Apmid%2F14021668&rft.aulast=Cleland&rft.aufirst=WW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-15"><a href="#cite_ref-15">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBergTymoczkoStryer2002" class="citation book cs1">Berg J, Tymoczko J, Stryer L (2002). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/bv.fcgi?call=bv.View..ShowTOC&rid=stryer.TOC&depth=2">Biochemistry</a>. W. H. Freeman and Company. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-7167-4955-4" title="Special:BookSources/978-0-7167-4955-4"><bdi>978-0-7167-4955-4</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20090926163540/http://www.ncbi.nlm.nih.gov/books/bv.fcgi?call=bv.View..ShowTOC&rid=stryer.TOC&depth=2">Archived</a> from the original on 26 September 2009. Retrieved 31 August 2017.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemistry&rft.pub=W.+H.+Freeman+and+Company&rft.date=2002&rft.isbn=978-0-7167-4955-4&rft.aulast=Berg&rft.aufirst=J&rft.au=Tymoczko%2C+J&rft.au=Stryer%2C+L&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2Fbv.fcgi%3Fcall%3Dbv.View..ShowTOC%26rid%3Dstryer.TOC%26depth%3D2&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-NIH_CTT-16">^ <a href="#cite_ref-NIH_CTT_16-0">a</a> <a href="#cite_ref-NIH_CTT_16-1">b</a> <a href="#cite_ref-NIH_CTT_16-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://web.archive.org/web/20110908030859/http://assay.nih.gov/assay/index.php/Types_of_Inhibition">"Types of Inhibition"</a>. NIH Center for Translational Therapeutics. Archived from <a rel="nofollow" class="external text" href="https://assay.nih.gov/assay/index.php/Types_of_Inhibition">the original</a> on 8 September 2011. Retrieved 2 April 2012.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=Types+of+Inhibition&rft.pub=NIH+Center+for+Translational+Therapeutics&rft_id=https%3A%2F%2Fassay.nih.gov%2Fassay%2Findex.php%2FTypes_of_Inhibition&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Cornish-Bowden_2012-17">^ <a href="#cite_ref-Cornish-Bowden_2012_17-0">a</a> <a href="#cite_ref-Cornish-Bowden_2012_17-1">b</a> <a href="#cite_ref-Cornish-Bowden_2012_17-2">c</a> <a href="#cite_ref-Cornish-Bowden_2012_17-3">d</a> <a href="#cite_ref-Cornish-Bowden_2012_17-4">e</a> <a href="#cite_ref-Cornish-Bowden_2012_17-5">f</a> <a href="#cite_ref-Cornish-Bowden_2012_17-6">g</a> <a href="#cite_ref-Cornish-Bowden_2012_17-7">h</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCornish-Bowden2012" class="citation book cs1">Cornish-Bowden A (2012). Fundamentals of Enzyme Kinetics (4th ed.). Weinheim: Wiley-VCH. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-527-66549-5" title="Special:BookSources/978-3-527-66549-5"><bdi>978-3-527-66549-5</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Fundamentals+of+Enzyme+Kinetics&rft.place=Weinheim&rft.edition=4th&rft.pub=Wiley-VCH&rft.date=2012&rft.isbn=978-3-527-66549-5&rft.aulast=Cornish-Bowden&rft.aufirst=A&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Segel-18">^ <a href="#cite_ref-Segel_18-0">a</a> <a href="#cite_ref-Segel_18-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSegel1993" class="citation book cs1">Segel IH (1993). Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (New ed.). Wiley-Interscience. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-471-30309-1" title="Special:BookSources/978-0-471-30309-1"><bdi>978-0-471-30309-1</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Enzyme+Kinetics%3A+Behavior+and+Analysis+of+Rapid+Equilibrium+and+Steady-State+Enzyme+Systems&rft.edition=New&rft.pub=Wiley-Interscience&rft.date=1993&rft.isbn=978-0-471-30309-1&rft.aulast=Segel&rft.aufirst=IH&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Palmer_2007-19"><a href="#cite_ref-Palmer_2007_19-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPalmerBonner2007" class="citation book cs1">Palmer T, Bonner PL (2007). "Enzyme inhibition.". Enzymes: Biochemistry, Biotechnology, Clinical Chemistry (2nd ed.). Woodhead Publishing. pp. 126–152 (135). <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1533%2F9780857099921.2.126">10.1533/9780857099921.2.126</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-904275-27-5" title="Special:BookSources/978-1-904275-27-5"><bdi>978-1-904275-27-5</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Enzyme+inhibition.&rft.btitle=Enzymes%3A+Biochemistry%2C+Biotechnology%2C+Clinical+Chemistry&rft.pages=126-152+%28135%29&rft.edition=2nd&rft.pub=Woodhead+Publishing&rft.date=2007&rft_id=info%3Adoi%2F10.1533%2F9780857099921.2.126&rft.isbn=978-1-904275-27-5&rft.aulast=Palmer&rft.aufirst=T&rft.au=Bonner%2C+PL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Delaune_2021-20"><a href="#cite_ref-Delaune_2021_20-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDelauneAlsayouri2021" class="citation book cs1">Delaune KP, Alsayouri K (September 2021). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK545242/">"Physiology: Noncompetitive Inhibitor"</a>. StatPearls. Treasure Island (FL): StatPearls Publishing. p. 31424826. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/31424826">31424826</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20211128175329/https://www.ncbi.nlm.nih.gov/books/NBK545242/">Archived</a> from the original on 28 November 2021. Retrieved 3 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Physiology%3A+Noncompetitive+Inhibitor&rft.btitle=StatPearls&rft.place=Treasure+Island+%28FL%29&rft.pages=31424826&rft.pub=StatPearls+Publishing&rft.date=2021-09&rft_id=info%3Apmid%2F31424826&rft.aulast=Delaune&rft.aufirst=KP&rft.au=Alsayouri%2C+K&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK545242%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Voet_2016-21">^ <a href="#cite_ref-Voet_2016_21-0">a</a> <a href="#cite_ref-Voet_2016_21-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFVoetVoetPratt2016" class="citation book cs1">Voet D, Voet JG, Pratt CW (2016). "Chapter 12: Enzyme Kinetics, Inhibition, and Control". Fundamentals of Biochemistry: Life at the Molecular Level (Fifth ed.). Hoboken, NJ: Wiley. pp. 361–401. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-118-91840-1" title="Special:BookSources/978-1-118-91840-1"><bdi>978-1-118-91840-1</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+12%3A+Enzyme+Kinetics%2C+Inhibition%2C+and+Control&rft.btitle=Fundamentals+of+Biochemistry%3A+Life+at+the+Molecular+Level&rft.place=Hoboken%2C+NJ&rft.pages=%3Cspan+class%3D%22nowrap%22%3E361-%3C%2Fspan%3E401&rft.edition=Fifth&rft.pub=Wiley&rft.date=2016&rft.isbn=978-1-118-91840-1&rft.aulast=Voet&rft.aufirst=D&rft.au=Voet%2C+JG&rft.au=Pratt%2C+CW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Buker_2019-22"><a href="#cite_ref-Buker_2019_22-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBukerBoriack-SjodinCopeland2019" class="citation journal cs1">Buker SM, Boriack-Sjodin PA, Copeland RA (June 2019). <a rel="nofollow" class="external text" href="https://doi.org/10.1177%2F2472555219829898">"Enzyme-Inhibitor Interactions and a Simple, Rapid Method for Determining Inhibition Modality"</a>. SLAS Discovery: Advancing Life Sciences R & D. 24 (5): 515–522 (516). <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1177%2F2472555219829898">10.1177/2472555219829898</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30811960">30811960</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:73480979">73480979</a>. <q>In some cases, the inhibitor may bind to a distinct site on the enzyme that is in allosteric communication with the substrate binding pocket. In many cases, allosteric, substrate competitive compounds result in conformational changes to the enzyme that change the ability of the enzyme to bind substrate.</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=SLAS+Discovery%3A+Advancing+Life+Sciences+R+%26+D&rft.atitle=Enzyme-Inhibitor+Interactions+and+a+Simple%2C+Rapid+Method+for+Determining+Inhibition+Modality&rft.volume=24&rft.issue=5&rft.pages=515-522+%28516%29&rft.date=2019-06&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A73480979%23id-name%3DS2CID&rft_id=info%3Apmid%2F30811960&rft_id=info%3Adoi%2F10.1177%2F2472555219829898&rft.aulast=Buker&rft.aufirst=SM&rft.au=Boriack-Sjodin%2C+PA&rft.au=Copeland%2C+RA&rft_id=https%3A%2F%2Fdoi.org%2F10.1177%252F2472555219829898&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-23"><a href="#cite_ref-23">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLaidler1978" class="citation book cs1">Laidler KJ (1978). Physical Chemistry with Biological Applications. Benjamin/Cummings. p. 437. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-8053-5680-9" title="Special:BookSources/978-0-8053-5680-9"><bdi>978-0-8053-5680-9</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Physical+Chemistry+with+Biological+Applications&rft.pages=437&rft.pub=Benjamin%2FCummings&rft.date=1978&rft.isbn=978-0-8053-5680-9&rft.aulast=Laidler&rft.aufirst=KJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Bisswanger_2017-24">^ <a href="#cite_ref-Bisswanger_2017_24-0">a</a> <a href="#cite_ref-Bisswanger_2017_24-1">b</a> <a href="#cite_ref-Bisswanger_2017_24-2">c</a> <a href="#cite_ref-Bisswanger_2017_24-3">d</a> <a href="#cite_ref-Bisswanger_2017_24-4">e</a> <a href="#cite_ref-Bisswanger_2017_24-5">f</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBisswanger2017" class="citation book cs1">Bisswanger H (2017). Enzyme Kinetics: Principles and Methods (3rd ed.). Newark: John Wiley & Sons, Incorporated. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-527-80647-8" title="Special:BookSources/978-3-527-80647-8"><bdi>978-3-527-80647-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Enzyme+Kinetics%3A+Principles+and+Methods.&rft.place=Newark&rft.edition=3rd&rft.pub=John+Wiley+%26+Sons%2C+Incorporated&rft.date=2017&rft.isbn=978-3-527-80647-8&rft.aulast=Bisswanger&rft.aufirst=H&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Marangoni_2003-25"><a href="#cite_ref-Marangoni_2003_25-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMarangoni2003" class="citation book cs1">Marangoni AG (2003). "Reversible Enzyme Inhibition". Enzyme Kinetics: A Modern Approach. Hoboken, N.J.: Wiley-Interscience. pp. 61–69. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-471-15985-8" title="Special:BookSources/978-0-471-15985-8"><bdi>978-0-471-15985-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Reversible+Enzyme+Inhibition&rft.btitle=Enzyme+Kinetics%3A+A+Modern+Approach&rft.place=Hoboken%2C+N.J.&rft.pages=%3Cspan+class%3D%22nowrap%22%3E61-%3C%2Fspan%3E69&rft.pub=Wiley-Interscience&rft.date=2003&rft.isbn=978-0-471-15985-8&rft.aulast=Marangoni&rft.aufirst=AG&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-26"><a href="#cite_ref-26">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSegel1993" class="citation book cs1">Segel IH (1993). Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (New ed.). Wiley–Interscience. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-471-30309-1" title="Special:BookSources/978-0-471-30309-1"><bdi>978-0-471-30309-1</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Enzyme+Kinetics%3A+Behavior+and+Analysis+of+Rapid+Equilibrium+and+Steady-State+Enzyme+Systems&rft.edition=New&rft.pub=Wiley%E2%80%93Interscience&rft.date=1993&rft.isbn=978-0-471-30309-1&rft.aulast=Segel&rft.aufirst=IH&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Walsh_2021-27">^ <a href="#cite_ref-Walsh_2021_27-0">a</a> <a href="#cite_ref-Walsh_2021_27-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFWalshMartinDarvesh2011" class="citation journal cs1">Walsh R, Martin E, Darvesh S (December 2011). "Limitations of conventional inhibitor classifications". Integrative Biology. 3 (12): 1197–1201. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1039%2Fc1ib00053e">10.1039/c1ib00053e</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22038120">22038120</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Integrative+Biology&rft.atitle=Limitations+of+conventional+inhibitor+classifications&rft.volume=3&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1197-%3C%2Fspan%3E1201&rft.date=2011-12&rft_id=info%3Adoi%2F10.1039%2Fc1ib00053e&rft_id=info%3Apmid%2F22038120&rft.aulast=Walsh&rft.aufirst=R&rft.au=Martin%2C+E&rft.au=Darvesh%2C+S&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Walsh_2007-28">^ <a href="#cite_ref-Walsh_2007_28-0">a</a> <a href="#cite_ref-Walsh_2007_28-1">b</a> <a href="#cite_ref-Walsh_2007_28-2">c</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFWalshMartinDarvesh2007" class="citation journal cs1">Walsh R, Martin E, Darvesh S (May 2007). "A versatile equation to describe reversible enzyme inhibition and activation kinetics: modeling beta-galactosidase and butyrylcholinesterase". Biochimica et Biophysica Acta (BBA) - General Subjects. 1770 (5): 733–746. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbagen.2007.01.001">10.1016/j.bbagen.2007.01.001</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17307293">17307293</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+General+Subjects&rft.atitle=A+versatile+equation+to+describe+reversible+enzyme+inhibition+and+activation+kinetics%3A+modeling+beta-galactosidase+and+butyrylcholinesterase&rft.volume=1770&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E733-%3C%2Fspan%3E746&rft.date=2007-05&rft_id=info%3Adoi%2F10.1016%2Fj.bbagen.2007.01.001&rft_id=info%3Apmid%2F17307293&rft.aulast=Walsh&rft.aufirst=R&rft.au=Martin%2C+E&rft.au=Darvesh%2C+S&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Walsh_2012-29"><a href="#cite_ref-Walsh_2012_29-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFWalsh2012" class="citation journal cs1">Walsh R (May 2012). "Alternative perspectives of enzyme kinetic modeling". Medicinal Chemistry and Drug Design. (16). InTech: 357–372.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Medicinal+Chemistry+and+Drug+Design.&rft.atitle=Alternative+perspectives+of+enzyme+kinetic+modeling.&rft.issue=16&rft.pages=%3Cspan+class%3D%22nowrap%22%3E357-%3C%2Fspan%3E372&rft.date=2012-05&rft.aulast=Walsh&rft.aufirst=R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Strelow_2012-30"><a href="#cite_ref-Strelow_2012_30-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFStrelowDeweIversenBrooks2012" class="citation book cs1">Strelow J, Dewe W, Iversen PW, Brooks PB, Radding JA, McGee J, et al. (October 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK92001/">"Mechanism of Action Assays for Enzymes"</a>. In Markossian S, Grossman A, Brimacombe K, et al. (eds.). Assay Guidance Manual. Eli Lilly & Company and the National Center for Advancing Translational Sciences. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22553872">22553872</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220615135104/http://www.ncbi.nlm.nih.gov/books/NBK92001/">Archived</a> from the original on 15 June 2022. Retrieved 9 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Mechanism+of+Action+Assays+for+Enzymes&rft.btitle=Assay+Guidance+Manual&rft.pub=Eli+Lilly+%26+Company+and+the+National+Center+for+Advancing+Translational+Sciences&rft.date=2012-10&rft_id=info%3Apmid%2F22553872&rft.aulast=Strelow&rft.aufirst=J&rft.au=Dewe%2C+W&rft.au=Iversen%2C+PW&rft.au=Brooks%2C+PB&rft.au=Radding%2C+JA&rft.au=McGee%2C+J&rft.au=Weidner%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK92001%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-31"><a href="#cite_ref-31">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHoldgate2001" class="citation journal cs1">Holdgate GA (July 2001). "Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics". BioTechniques. 31 (1): 164–6, 168, 170 passim. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11464510">11464510</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=BioTechniques&rft.atitle=Making+cool+drugs+hot%3A+isothermal+titration+calorimetry+as+a+tool+to+study+binding+energetics&rft.volume=31&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E164-%3C%2Fspan%3E6%2C+168%2C+170+passim&rft.date=2001-07&rft_id=info%3Apmid%2F11464510&rft.aulast=Holdgate&rft.aufirst=GA&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-32"><a href="#cite_ref-32">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLeatherbarrow1990" class="citation journal cs1">Leatherbarrow RJ (December 1990). "Using linear and non-linear regression to fit biochemical data". Trends in Biochemical Sciences. 15 (12): 455–458. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0968-0004%2890%2990295-M">10.1016/0968-0004(90)90295-M</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2077683">2077683</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Biochemical+Sciences&rft.atitle=Using+linear+and+non-linear+regression+to+fit+biochemical+data&rft.volume=15&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E455-%3C%2Fspan%3E458&rft.date=1990-12&rft_id=info%3Adoi%2F10.1016%2F0968-0004%2890%2990295-M&rft_id=info%3Apmid%2F2077683&rft.aulast=Leatherbarrow&rft.aufirst=RJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Tseng_1990-33">^ <a href="#cite_ref-Tseng_1990_33-0">a</a> <a href="#cite_ref-Tseng_1990_33-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTsengHsu1990" class="citation journal cs1">Tseng SJ, Hsu JP (August 1990). "A comparison of the parameter estimating procedures for the Michaelis-Menten model". Journal of Theoretical Biology. 145 (4): 457–464. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1990JThBi.145..457T">1990JThBi.145..457T</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0022-5193%2805%2980481-3">10.1016/S0022-5193(05)80481-3</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2246896">2246896</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Theoretical+Biology&rft.atitle=A+comparison+of+the+parameter+estimating+procedures+for+the+Michaelis-Menten+model&rft.volume=145&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E457-%3C%2Fspan%3E464&rft.date=1990-08&rft_id=info%3Apmid%2F2246896&rft_id=info%3Adoi%2F10.1016%2FS0022-5193%2805%2980481-3&rft_id=info%3Abibcode%2F1990JThBi.145..457T&rft.aulast=Tseng&rft.aufirst=SJ&rft.au=Hsu%2C+JP&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-34"><a href="#cite_ref-34">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDixonWebbThorneTipton1979" class="citation book cs1">Dixon M, Webb EC, Thorne CJ, Tipton KF (1979). Enzymes (3rd ed.). London: Longman. p. 126. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-470-20745-1" title="Special:BookSources/978-0-470-20745-1"><bdi>978-0-470-20745-1</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Enzymes&rft.place=London&rft.pages=126&rft.edition=3rd&rft.pub=Longman&rft.date=1979&rft.isbn=978-0-470-20745-1&rft.aulast=Dixon&rft.aufirst=M&rft.au=Webb%2C+EC&rft.au=Thorne%2C+CJ&rft.au=Tipton%2C+KF&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-35"><a href="#cite_ref-35">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRadzickaWolfenden1995" class="citation book cs1">Radzicka A, Wolfenden R (1995). "Transition state and multisubstrate analog inhibitors". Enzyme Kinetics and Mechanism Part D: Developments in Enzyme Dynamics. Methods in Enzymology. Vol. 249. pp. 284–312. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0076-6879%2895%2949039-6">10.1016/0076-6879(95)49039-6</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9780121821500" title="Special:BookSources/9780121821500"><bdi>9780121821500</bdi></a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7791615">7791615</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Transition+state+and+multisubstrate+analog+inhibitors&rft.btitle=Enzyme+Kinetics+and+Mechanism+Part+D%3A+Developments+in+Enzyme+Dynamics&rft.series=Methods+in+Enzymology&rft.pages=%3Cspan+class%3D%22nowrap%22%3E284-%3C%2Fspan%3E312&rft.date=1995&rft_id=info%3Apmid%2F7791615&rft_id=info%3Adoi%2F10.1016%2F0076-6879%2895%2949039-6&rft.isbn=9780121821500&rft.aulast=Radzicka&rft.aufirst=A&rft.au=Wolfenden%2C+R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-36"><a href="#cite_ref-36">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSchifferBurkeBesarabLasker1977" class="citation journal cs1">Schiffer CF, Burke JF, Besarab A, Lasker N, Simenhoff ML (January 1977). "Amylase/creatinine clearance fraction in patients on chronic hemodialysis". Annals of Internal Medicine. 86 (1): 65–66. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.7326%2F0003-4819-86-1-65">10.7326/0003-4819-86-1-65</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/319722">319722</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annals+of+Internal+Medicine&rft.atitle=Amylase%2Fcreatinine+clearance+fraction+in+patients+on+chronic+hemodialysis&rft.volume=86&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E65-%3C%2Fspan%3E66&rft.date=1977-01&rft_id=info%3Adoi%2F10.7326%2F0003-4819-86-1-65&rft_id=info%3Apmid%2F319722&rft.aulast=Schiffer&rft.aufirst=CF&rft.au=Burke%2C+JF&rft.au=Besarab%2C+A&rft.au=Lasker%2C+N&rft.au=Simenhoff%2C+ML&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-37"><a href="#cite_ref-37">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFIngleseBlatchlyBenkovic1989" class="citation journal cs1">Inglese J, Blatchly RA, Benkovic SJ (May 1989). "A multisubstrate adduct inhibitor of a purine biosynthetic enzyme with a picomolar dissociation constant". Journal of Medicinal Chemistry. 32 (5): 937–940. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fjm00125a002">10.1021/jm00125a002</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2709379">2709379</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Medicinal+Chemistry&rft.atitle=A+multisubstrate+adduct+inhibitor+of+a+purine+biosynthetic+enzyme+with+a+picomolar+dissociation+constant&rft.volume=32&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E937-%3C%2Fspan%3E940&rft.date=1989-05&rft_id=info%3Adoi%2F10.1021%2Fjm00125a002&rft_id=info%3Apmid%2F2709379&rft.aulast=Inglese&rft.aufirst=J&rft.au=Blatchly%2C+RA&rft.au=Benkovic%2C+SJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-38"><a href="#cite_ref-38">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFIngleseBenkovic1991" class="citation journal cs1">Inglese J, Benkovic SJ (1991). "Multisubstrate Adduct Inhibitors of Glycinamide Ribonucleotide Transformylase: Synthetic and Enzyme Generated". Tetrahedron. 47 (14–15): 2351–2364. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0040-4020%2801%2981773-7">10.1016/S0040-4020(01)81773-7</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Tetrahedron&rft.atitle=Multisubstrate+Adduct+Inhibitors+of+Glycinamide+Ribonucleotide+Transformylase%3A+Synthetic+and+Enzyme+Generated.&rft.volume=47&rft.issue=%3Cspan+class%3D%22nowrap%22%3E14%E2%80%93%3C%2Fspan%3E15&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2351-%3C%2Fspan%3E2364&rft.date=1991&rft_id=info%3Adoi%2F10.1016%2FS0040-4020%2801%2981773-7&rft.aulast=Inglese&rft.aufirst=J&rft.au=Benkovic%2C+SJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-39"><a href="#cite_ref-39">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRozwarskiGrantBartonJacobs1998" class="citation journal cs1">Rozwarski DA, Grant GA, Barton DH, Jacobs WR, Sacchettini JC (January 1998). "Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis". Science. 279 (5347): 98–102. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1998Sci...279...98R">1998Sci...279...98R</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.279.5347.98">10.1126/science.279.5347.98</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9417034">9417034</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Science&rft.atitle=Modification+of+the+NADH+of+the+isoniazid+target+%28InhA%29+from+Mycobacterium+tuberculosis&rft.volume=279&rft.issue=5347&rft.pages=%3Cspan+class%3D%22nowrap%22%3E98-%3C%2Fspan%3E102&rft.date=1998-01&rft_id=info%3Apmid%2F9417034&rft_id=info%3Adoi%2F10.1126%2Fscience.279.5347.98&rft_id=info%3Abibcode%2F1998Sci...279...98R&rft.aulast=Rozwarski&rft.aufirst=DA&rft.au=Grant%2C+GA&rft.au=Barton%2C+DH&rft.au=Jacobs%2C+WR&rft.au=Sacchettini%2C+JC&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-40"><a href="#cite_ref-40">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFAuldLovellThorneLea2010" class="citation journal cs1">Auld DS, Lovell S, Thorne N, Lea WA, Maloney DJ, Shen M, et al. (March 2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2841876">"Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124"</a>. Proceedings of the National Academy of Sciences of the United States of America. 107 (11): 4878–4883. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2010PNAS..107.4878A">2010PNAS..107.4878A</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.0909141107">10.1073/pnas.0909141107</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2841876">2841876</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20194791">20194791</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&rft.atitle=Molecular+basis+for+the+high-affinity+binding+and+stabilization+of+firefly+luciferase+by+PTC124&rft.volume=107&rft.issue=11&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4878-%3C%2Fspan%3E4883&rft.date=2010-03&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2841876%23id-name%3DPMC&rft_id=info%3Apmid%2F20194791&rft_id=info%3Adoi%2F10.1073%2Fpnas.0909141107&rft_id=info%3Abibcode%2F2010PNAS..107.4878A&rft.aulast=Auld&rft.aufirst=DS&rft.au=Lovell%2C+S&rft.au=Thorne%2C+N&rft.au=Lea%2C+WA&rft.au=Maloney%2C+DJ&rft.au=Shen%2C+M&rft.au=Rai%2C+G&rft.au=Battaile%2C+KP&rft.au=Thomas%2C+CJ&rft.au=Simeonov%2C+A&rft.au=Hanzlik%2C+RP&rft.au=Inglese%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2841876&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Le_Calvez_2009-41"><a href="#cite_ref-Le_Calvez_2009_41-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLe_CalvezScottMigaud2009" class="citation journal cs1">Le Calvez PB, Scott CJ, Migaud ME (December 2009). "Multisubstrate adduct inhibitors: drug design and biological tools". Journal of Enzyme Inhibition and Medicinal Chemistry. 24 (6): 1291–318. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3109%2F14756360902843809">10.3109/14756360902843809</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19912064">19912064</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:21808708">21808708</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Enzyme+Inhibition+and+Medicinal+Chemistry&rft.atitle=Multisubstrate+adduct+inhibitors%3A+drug+design+and+biological+tools&rft.volume=24&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1291-%3C%2Fspan%3E318&rft.date=2009-12&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A21808708%23id-name%3DS2CID&rft_id=info%3Apmid%2F19912064&rft_id=info%3Adoi%2F10.3109%2F14756360902843809&rft.aulast=Le+Calvez&rft.aufirst=PB&rft.au=Scott%2C+CJ&rft.au=Migaud%2C+ME&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Avendano_2015-42">^ <a href="#cite_ref-Avendano_2015_42-0">a</a> <a href="#cite_ref-Avendano_2015_42-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFAvendanoMenendez2015" class="citation book cs1">Avendano C, Menendez JC (June 2015). "Chapter 2.5: Inhibitors of Dihydrofolate Reductase". Medicinal Chemistry of Anticancer Drugs. Elsevier. pp. 54–58. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-444-62667-7" title="Special:BookSources/978-0-444-62667-7"><bdi>978-0-444-62667-7</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+2.5%3A+Inhibitors+of+Dihydrofolate+Reductase&rft.btitle=Medicinal+Chemistry+of+Anticancer+Drugs&rft.pages=%3Cspan+class%3D%22nowrap%22%3E54-%3C%2Fspan%3E58&rft.pub=Elsevier&rft.date=2015-06&rft.isbn=978-0-444-62667-7&rft.aulast=Avendano&rft.aufirst=C&rft.au=Menendez%2C+JC&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-43"><a href="#cite_ref-43">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHsuWangChenShih2006" class="citation journal cs1">Hsu JT, Wang HC, Chen GW, Shih SR (2006). "Antiviral drug discovery targeting to viral proteases". Current Pharmaceutical Design. 12 (11): 1301–1314. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F138161206776361110">10.2174/138161206776361110</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16611117">16611117</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Pharmaceutical+Design&rft.atitle=Antiviral+drug+discovery+targeting+to+viral+proteases&rft.volume=12&rft.issue=11&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1301-%3C%2Fspan%3E1314&rft.date=2006&rft_id=info%3Adoi%2F10.2174%2F138161206776361110&rft_id=info%3Apmid%2F16611117&rft.aulast=Hsu&rft.aufirst=JT&rft.au=Wang%2C+HC&rft.au=Chen%2C+GW&rft.au=Shih%2C+SR&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Agbowuro_2018-44"><a href="#cite_ref-Agbowuro_2018_44-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFAgbowuroHustonGambleTyndall2018" class="citation journal cs1">Agbowuro AA, Huston WM, Gamble AB, Tyndall JD (July 2018). "Proteases and protease inhibitors in infectious diseases". Medicinal Research Reviews. 38 (4): 1295–1331. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fmed.21475">10.1002/med.21475</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29149530">29149530</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:25269012">25269012</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Medicinal+Research+Reviews&rft.atitle=Proteases+and+protease+inhibitors+in+infectious+diseases&rft.volume=38&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1295-%3C%2Fspan%3E1331&rft.date=2018-07&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A25269012%23id-name%3DS2CID&rft_id=info%3Apmid%2F29149530&rft_id=info%3Adoi%2F10.1002%2Fmed.21475&rft.aulast=Agbowuro&rft.aufirst=AA&rft.au=Huston%2C+WM&rft.au=Gamble%2C+AB&rft.au=Tyndall%2C+JD&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Qiu_2011-45"><a href="#cite_ref-Qiu_2011_45-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFQiuLiu2011" class="citation journal cs1">Qiu X, Liu ZP (2011). "Recent developments of peptidomimetic HIV-1 protease inhibitors". Current Medicinal Chemistry. 18 (29): 4513–37. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F092986711797287566">10.2174/092986711797287566</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21864279">21864279</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Medicinal+Chemistry&rft.atitle=Recent+developments+of+peptidomimetic+HIV-1+protease+inhibitors&rft.volume=18&rft.issue=29&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4513-%3C%2Fspan%3E37&rft.date=2011&rft_id=info%3Adoi%2F10.2174%2F092986711797287566&rft_id=info%3Apmid%2F21864279&rft.aulast=Qiu&rft.aufirst=X&rft.au=Liu%2C+ZP&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Schramm_2018-46">^ <a href="#cite_ref-Schramm_2018_46-0">a</a> <a href="#cite_ref-Schramm_2018_46-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSchramm2018" class="citation journal cs1">Schramm VL (November 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6615489">"Enzymatic Transition States and Drug Design"</a>. Chemical Reviews. 118 (22): 11194–11258. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Facs.chemrev.8b00369">10.1021/acs.chemrev.8b00369</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6615489">6615489</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30335982">30335982</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Reviews&rft.atitle=Enzymatic+Transition+States+and+Drug+Design&rft.volume=118&rft.issue=22&rft.pages=%3Cspan+class%3D%22nowrap%22%3E11194-%3C%2Fspan%3E11258&rft.date=2018-11&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6615489%23id-name%3DPMC&rft_id=info%3Apmid%2F30335982&rft_id=info%3Adoi%2F10.1021%2Facs.chemrev.8b00369&rft.aulast=Schramm&rft.aufirst=VL&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6615489&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-pmid10702632-47"><a href="#cite_ref-pmid10702632_47-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLewChenKim2000" class="citation journal cs1">Lew W, Chen X, Kim CU (June 2000). "Discovery and development of GS 4104 (oseltamivir): an orally active influenza neuraminidase inhibitor". Current Medicinal Chemistry. 7 (6): 663–672. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F0929867003374886">10.2174/0929867003374886</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10702632">10702632</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Medicinal+Chemistry&rft.atitle=Discovery+and+development+of+GS+4104+%28oseltamivir%29%3A+an+orally+active+influenza+neuraminidase+inhibitor&rft.volume=7&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E663-%3C%2Fspan%3E672&rft.date=2000-06&rft_id=info%3Adoi%2F10.2174%2F0929867003374886&rft_id=info%3Apmid%2F10702632&rft.aulast=Lew&rft.aufirst=W&rft.au=Chen%2C+X&rft.au=Kim%2C+CU&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-48"><a href="#cite_ref-48">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFischer2003" class="citation journal cs1">Fischer PM (October 2003). "The design, synthesis and application of stereochemical and directional peptide isomers: a critical review". Current Protein & Peptide Science. 4 (5): 339–356. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1389203033487054">10.2174/1389203033487054</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14529528">14529528</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Protein+%26+Peptide+Science&rft.atitle=The+design%2C+synthesis+and+application+of+stereochemical+and+directional+peptide+isomers%3A+a+critical+review&rft.volume=4&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E339-%3C%2Fspan%3E356&rft.date=2003-10&rft_id=info%3Adoi%2F10.2174%2F1389203033487054&rft_id=info%3Apmid%2F14529528&rft.aulast=Fischer&rft.aufirst=PM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Breen_2015-49"><a href="#cite_ref-Breen_2015_49-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBreenSoellner2015" class="citation journal cs1">Breen ME, Soellner MB (January 2015). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4301090">"Small molecule substrate phosphorylation site inhibitors of protein kinases: approaches and challenges"</a>. ACS Chemical Biology. 10 (1): 175–89. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fcb5008376">10.1021/cb5008376</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4301090">4301090</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/25494294">25494294</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=ACS+Chemical+Biology&rft.atitle=Small+molecule+substrate+phosphorylation+site+inhibitors+of+protein+kinases%3A+approaches+and+challenges&rft.volume=10&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E175-%3C%2Fspan%3E89&rft.date=2015-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4301090%23id-name%3DPMC&rft_id=info%3Apmid%2F25494294&rft_id=info%3Adoi%2F10.1021%2Fcb5008376&rft.aulast=Breen&rft.aufirst=ME&rft.au=Soellner%2C+MB&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4301090&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-50"><a href="#cite_ref-50">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBogoyevitchBarrKetterman2005" class="citation journal cs1">Bogoyevitch MA, Barr RK, Ketterman AJ (December 2005). "Peptide inhibitors of protein kinases-discovery, characterisation and use". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1754 (1–2): 79–99. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbapap.2005.07.025">10.1016/j.bbapap.2005.07.025</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16182621">16182621</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Proteins+and+Proteomics&rft.atitle=Peptide+inhibitors+of+protein+kinases-discovery%2C+characterisation+and+use&rft.volume=1754&rft.issue=%3Cspan+class%3D%22nowrap%22%3E1%E2%80%93%3C%2Fspan%3E2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E79-%3C%2Fspan%3E99&rft.date=2005-12&rft_id=info%3Adoi%2F10.1016%2Fj.bbapap.2005.07.025&rft_id=info%3Apmid%2F16182621&rft.aulast=Bogoyevitch&rft.aufirst=MA&rft.au=Barr%2C+RK&rft.au=Ketterman%2C+AJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Patrick_2017-51">^ <a href="#cite_ref-Patrick_2017_51-0">a</a> <a href="#cite_ref-Patrick_2017_51-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPatrick2017" class="citation book cs1">Patrick GL (2017). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=bBqeDgAAQBAJ&pg=PA95">"Enzymes as Drug Targets"</a>. An Introduction to Medicinal Chemistry (Sixth ed.). Oxford, United Kingdom: Oxford University Press. p. 95. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-19-874969-1" title="Special:BookSources/978-0-19-874969-1"><bdi>978-0-19-874969-1</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328010009/https://books.google.com/books?id=bBqeDgAAQBAJ&pg=PA95">Archived</a> from the original on 28 March 2023. Retrieved 3 June 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Enzymes+as+Drug+Targets&rft.btitle=An+Introduction+to+Medicinal+Chemistry&rft.place=Oxford%2C+United+Kingdom&rft.pages=95&rft.edition=Sixth&rft.pub=Oxford+University+Press&rft.date=2017&rft.isbn=978-0-19-874969-1&rft.aulast=Patrick&rft.aufirst=GL&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DbBqeDgAAQBAJ%26pg%3DPA95&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Gehringer_2019-52"><a href="#cite_ref-Gehringer_2019_52-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGehringerLaufer2019" class="citation journal cs1">Gehringer M, Laufer SA (June 2019). "Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology". Journal of Medicinal Chemistry. 62 (12): 5673–5724. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Facs.jmedchem.8b01153">10.1021/acs.jmedchem.8b01153</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30565923">30565923</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:56480231">56480231</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Medicinal+Chemistry&rft.atitle=Emerging+and+Re-Emerging+Warheads+for+Targeted+Covalent+Inhibitors%3A+Applications+in+Medicinal+Chemistry+and+Chemical+Biology&rft.volume=62&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5673-%3C%2Fspan%3E5724&rft.date=2019-06&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A56480231%23id-name%3DS2CID&rft_id=info%3Apmid%2F30565923&rft_id=info%3Adoi%2F10.1021%2Facs.jmedchem.8b01153&rft.aulast=Gehringer&rft.aufirst=M&rft.au=Laufer%2C+SA&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-53"><a href="#cite_ref-53">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLundblad2004" class="citation book cs1">Lundblad RL (2004). Chemical reagents for protein modification (3rd ed.). CRC Press. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-8493-1983-9" title="Special:BookSources/978-0-8493-1983-9"><bdi>978-0-8493-1983-9</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Chemical+reagents+for+protein+modification&rft.edition=3rd&rft.pub=CRC+Press&rft.date=2004&rft.isbn=978-0-8493-1983-9&rft.aulast=Lundblad&rft.aufirst=RL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-54"><a href="#cite_ref-54">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPolakovičVrabelBáleš1998" class="citation journal cs1">Polakovič M, Vrabel P, Báleš V (January 1998). "Approaches for improved identification of mechanisms of enzyme inactivation". Progress in Biotechnology. 15. Elsevier: 77–82. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0921-0423%2898%2980013-0">10.1016/S0921-0423(98)80013-0</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-444-82970-2" title="Special:BookSources/978-0-444-82970-2"><bdi>978-0-444-82970-2</bdi></a>. <q>Enzyme inactivation is generally explained as a chemical process involving several phenomena like aggregation, dissociation into subunits, or denaturation (conformational changes), which occur simultaneously during the inactivation of a specific enzyme.</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Progress+in+Biotechnology&rft.atitle=Approaches+for+improved+identification+of+mechanisms+of+enzyme+inactivation.&rft.volume=15&rft.pages=%3Cspan+class%3D%22nowrap%22%3E77-%3C%2Fspan%3E82&rft.date=1998-01&rft_id=info%3Adoi%2F10.1016%2FS0921-0423%2898%2980013-0&rft.isbn=978-0-444-82970-2&rft.aulast=Polakovi%C4%8D&rft.aufirst=M&rft.au=Vrabel%2C+P&rft.au=B%C3%A1le%C5%A1%2C+V&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-55"><a href="#cite_ref-55">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPriceHamesRickwood1996" class="citation book cs1">Price N, Hames B, Rickwood D (1996). Proteins LabFax. BIOS Scientific Publishers. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-564710-6" title="Special:BookSources/978-0-12-564710-6"><bdi>978-0-12-564710-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Proteins+LabFax&rft.pub=BIOS+Scientific+Publishers&rft.date=1996&rft.isbn=978-0-12-564710-6&rft.aulast=Price&rft.aufirst=N&rft.au=Hames%2C+B&rft.au=Rickwood%2C+D&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-56"><a href="#cite_ref-56">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFAdamCravattSorensen2001" class="citation journal cs1">Adam GC, Cravatt BF, Sorensen EJ (January 2001). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS1074-5521%2800%2990060-7">"Profiling the specific reactivity of the proteome with non-directed activity-based probes"</a>. Chemistry & Biology. 8 (1): 81–95. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS1074-5521%2800%2990060-7">10.1016/S1074-5521(00)90060-7</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11182321">11182321</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemistry+%26+Biology&rft.atitle=Profiling+the+specific+reactivity+of+the+proteome+with+non-directed+activity-based+probes&rft.volume=8&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E81-%3C%2Fspan%3E95&rft.date=2001-01&rft_id=info%3Adoi%2F10.1016%2FS1074-5521%2800%2990060-7&rft_id=info%3Apmid%2F11182321&rft.aulast=Adam&rft.aufirst=GC&rft.au=Cravatt%2C+BF&rft.au=Sorensen%2C+EJ&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252FS1074-5521%252800%252990060-7&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-57"><a href="#cite_ref-57">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMaurerFung2000" class="citation journal cs1">Maurer T, Fung HL (2000). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2751003">"Comparison of methods for analyzing kinetic data from mechanism-based enzyme inactivation: application to nitric oxide synthase"</a>. AAPS PharmSci. 2 (1): 68–77. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1208%2Fps020108">10.1208/ps020108</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2751003">2751003</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11741224">11741224</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=AAPS+PharmSci&rft.atitle=Comparison+of+methods+for+analyzing+kinetic+data+from+mechanism-based+enzyme+inactivation%3A+application+to+nitric+oxide+synthase&rft.volume=2&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E68-%3C%2Fspan%3E77&rft.date=2000&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2751003%23id-name%3DPMC&rft_id=info%3Apmid%2F11741224&rft_id=info%3Adoi%2F10.1208%2Fps020108&rft.aulast=Maurer&rft.aufirst=T&rft.au=Fung%2C+HL&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2751003&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-pmid10398927-58"><a href="#cite_ref-pmid10398927_58-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLooDeJohnDuStevenson1999" class="citation journal cs1">Loo JA, DeJohn DE, Du P, Stevenson TI, Ogorzalek Loo RR (July 1999). "Application of mass spectrometry for target identification and characterization". Medicinal Research Reviews. 19 (4): 307–319. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2F%28SICI%291098-1128%28199907%2919%3A4%3C307%3A%3AAID-MED4%3E3.0.CO%3B2-2">10.1002/(SICI)1098-1128(199907)19:4<307::AID-MED4>3.0.CO;2-2</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10398927">10398927</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:11766917">11766917</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Medicinal+Research+Reviews&rft.atitle=Application+of+mass+spectrometry+for+target+identification+and+characterization&rft.volume=19&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E307-%3C%2Fspan%3E319&rft.date=1999-07&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A11766917%23id-name%3DS2CID&rft_id=info%3Apmid%2F10398927&rft_id=info%3Adoi%2F10.1002%2F%28SICI%291098-1128%28199907%2919%3A4%3C307%3A%3AAID-MED4%3E3.0.CO%3B2-2&rft.aulast=Loo&rft.aufirst=JA&rft.au=DeJohn%2C+DE&rft.au=Du%2C+P&rft.au=Stevenson%2C+TI&rft.au=Ogorzalek+Loo%2C+RR&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-59"><a href="#cite_ref-59">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPurich2010" class="citation book cs1">Purich DL (2010). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=SkSQNNACcrYC&dq=irreversible+enzyme+inhibitor+MALDI-TOF&pg=PA542">"Irreversible Enzyme Inhibition by Affinity Labelling Agents"</a>. Enzyme Kinetics: Catalysis and Control: A Reference of Theory and Best-Practice Methods. San Diego, Calif.: Elsevier Academic. p. 542. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-380925-4" title="Special:BookSources/978-0-12-380925-4"><bdi>978-0-12-380925-4</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220720192921/https://books.google.com/books?id=SkSQNNACcrYC&dq=irreversible+enzyme+inhibitor+MALDI-TOF&pg=PA542">Archived</a> from the original on 20 July 2022. Retrieved 20 July 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Irreversible+Enzyme+Inhibition+by+Affinity+Labelling+Agents&rft.btitle=Enzyme+Kinetics%3A+Catalysis+and+Control%3A+A+Reference+of+Theory+and+Best-Practice+Methods&rft.place=San+Diego%2C+Calif.&rft.pages=542&rft.pub=Elsevier+Academic&rft.date=2010&rft.isbn=978-0-12-380925-4&rft.aulast=Purich&rft.aufirst=DL&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DSkSQNNACcrYC%26dq%3Dirreversible%2Benzyme%2Binhibitor%2BMALDI-TOF%26pg%3DPA542&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Sibille_2012-60"><a href="#cite_ref-Sibille_2012_60-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSibilleBanaChaouniDiederich2012" class="citation journal cs1">Sibille E, Bana E, Chaouni W, Diederich M, Bagrel D, Chaimbault P (November 2012). "Development of a matrix-assisted laser desorption/ionization-mass spectrometry screening test to evidence reversible and irreversible inhibitors of CDC25 phosphatases". Analytical Biochemistry. 430 (1): 83–91. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ab.2012.08.006">10.1016/j.ab.2012.08.006</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22902804">22902804</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Analytical+Biochemistry&rft.atitle=Development+of+a+matrix-assisted+laser+desorption%2Fionization-mass+spectrometry+screening+test+to+evidence+reversible+and+irreversible+inhibitors+of+CDC25+phosphatases&rft.volume=430&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E83-%3C%2Fspan%3E91&rft.date=2012-11&rft_id=info%3Adoi%2F10.1016%2Fj.ab.2012.08.006&rft_id=info%3Apmid%2F22902804&rft.aulast=Sibille&rft.aufirst=E&rft.au=Bana%2C+E&rft.au=Chaouni%2C+W&rft.au=Diederich%2C+M&rft.au=Bagrel%2C+D&rft.au=Chaimbault%2C+P&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Poulin-61">^ <a href="#cite_ref-Poulin_61-0">a</a> <a href="#cite_ref-Poulin_61-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPoulinLuAckermannBey1992" class="citation journal cs1">Poulin R, Lu L, Ackermann B, Bey P, Pegg AE (January 1992). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0021-9258%2818%2948472-4">"Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites"</a>. The Journal of Biological Chemistry. 267 (1): 150–158. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0021-9258%2818%2948472-4">10.1016/S0021-9258(18)48472-4</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/1730582">1730582</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Mechanism+of+the+irreversible+inactivation+of+mouse+ornithine+decarboxylase+by+alpha-difluoromethylornithine.+Characterization+of+sequences+at+the+inhibitor+and+coenzyme+binding+sites&rft.volume=267&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E150-%3C%2Fspan%3E158&rft.date=1992-01&rft_id=info%3Adoi%2F10.1016%2FS0021-9258%2818%2948472-4&rft_id=info%3Apmid%2F1730582&rft.aulast=Poulin&rft.aufirst=R&rft.au=Lu%2C+L&rft.au=Ackermann%2C+B&rft.au=Bey%2C+P&rft.au=Pegg%2C+AE&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252FS0021-9258%252818%252948472-4&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-62"><a href="#cite_ref-62">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSzedlacsekDuggleby1995" class="citation book cs1">Szedlacsek SE, Duggleby RG (1995). "[6] Kinetics of slow and tight-binding inhibitors". Kinetics of slow and tight-binding inhibitors. Methods in Enzymology. Vol. 249. pp. 144–80. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0076-6879%2895%2949034-5">10.1016/0076-6879(95)49034-5</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-182150-0" title="Special:BookSources/978-0-12-182150-0"><bdi>978-0-12-182150-0</bdi></a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7791610">7791610</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=%26%2391%3B6%26%2393%3B+Kinetics+of+slow+and+tight-binding+inhibitors&rft.btitle=Kinetics+of+slow+and+tight-binding+inhibitors&rft.series=Methods+in+Enzymology&rft.pages=%3Cspan+class%3D%22nowrap%22%3E144-%3C%2Fspan%3E80&rft.date=1995&rft_id=info%3Apmid%2F7791610&rft_id=info%3Adoi%2F10.1016%2F0076-6879%2895%2949034-5&rft.isbn=978-0-12-182150-0&rft.aulast=Szedlacsek&rft.aufirst=SE&rft.au=Duggleby%2C+RG&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-63"><a href="#cite_ref-63">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFStoneMorrison1986" class="citation journal cs1">Stone SR, Morrison JF (February 1986). "Mechanism of inhibition of dihydrofolate reductases from bacterial and vertebrate sources by various classes of folate analogs". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 869 (3): 275–285. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0167-4838%2886%2990067-1">10.1016/0167-4838(86)90067-1</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/3511964">3511964</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Protein+Structure+and+Molecular+Enzymology&rft.atitle=Mechanism+of+inhibition+of+dihydrofolate+reductases+from+bacterial+and+vertebrate+sources+by+various+classes+of+folate+analogs&rft.volume=869&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E275-%3C%2Fspan%3E285&rft.date=1986-02&rft_id=info%3Adoi%2F10.1016%2F0167-4838%2886%2990067-1&rft_id=info%3Apmid%2F3511964&rft.aulast=Stone&rft.aufirst=SR&rft.au=Morrison%2C+JF&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-64"><a href="#cite_ref-64">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPickMcGartollBray1971" class="citation journal cs1">Pick FM, McGartoll MA, Bray RC (January 1971). <a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1432-1033.1971.tb01215.x">"Reaction of formaldehyde and of methanol with xanthine oxidase"</a>. European Journal of Biochemistry. 18 (1): 65–72. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1432-1033.1971.tb01215.x">10.1111/j.1432-1033.1971.tb01215.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/4322209">4322209</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=European+Journal+of+Biochemistry&rft.atitle=Reaction+of+formaldehyde+and+of+methanol+with+xanthine+oxidase&rft.volume=18&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E65-%3C%2Fspan%3E72&rft.date=1971-01&rft_id=info%3Adoi%2F10.1111%2Fj.1432-1033.1971.tb01215.x&rft_id=info%3Apmid%2F4322209&rft.aulast=Pick&rft.aufirst=FM&rft.au=McGartoll%2C+MA&rft.au=Bray%2C+RC&rft_id=https%3A%2F%2Fdoi.org%2F10.1111%252Fj.1432-1033.1971.tb01215.x&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-65"><a href="#cite_ref-65">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFReardon1989" class="citation journal cs1">Reardon JE (November 1989). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0021-9258%2819%2947263-3">"Herpes simplex virus type 1 and human DNA polymerase interactions with 2'-deoxyguanosine 5'-triphosphate analogs. Kinetics of incorporation into DNA and induction of inhibition"</a>. The Journal of Biological Chemistry. 264 (32): 19039–19044. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0021-9258%2819%2947263-3">10.1016/S0021-9258(19)47263-3</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2553730">2553730</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Herpes+simplex+virus+type+1+and+human+DNA+polymerase+interactions+with+2%27-deoxyguanosine+5%27-triphosphate+analogs.+Kinetics+of+incorporation+into+DNA+and+induction+of+inhibition&rft.volume=264&rft.issue=32&rft.pages=%3Cspan+class%3D%22nowrap%22%3E19039-%3C%2Fspan%3E19044&rft.date=1989-11&rft_id=info%3Adoi%2F10.1016%2FS0021-9258%2819%2947263-3&rft_id=info%3Apmid%2F2553730&rft.aulast=Reardon&rft.aufirst=JE&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252FS0021-9258%252819%252947263-3&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-pmid15102853-66"><a href="#cite_ref-pmid15102853_66-0">^</a> <a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a>: <a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1GXF">1GXF</a>; <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSaravanamuthuVickersBondPeterson2004" class="citation journal cs1">Saravanamuthu A, Vickers TJ, Bond CS, Peterson MR, Hunter WN, Fairlamb AH (July 2004). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3491871">"Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design"</a>. The Journal of Biological Chemistry. 279 (28): 29493–500. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M403187200">10.1074/jbc.M403187200</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3491871">3491871</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15102853">15102853</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Two+interacting+binding+sites+for+quinacrine+derivatives+in+the+active+site+of+trypanothione+reductase%3A+a+template+for+drug+design&rft.volume=279&rft.issue=28&rft.pages=%3Cspan+class%3D%22nowrap%22%3E29493-%3C%2Fspan%3E500&rft.date=2004-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3491871%23id-name%3DPMC&rft_id=info%3Apmid%2F15102853&rft_id=info%3Adoi%2F10.1074%2Fjbc.M403187200&rft.aulast=Saravanamuthu&rft.aufirst=A&rft.au=Vickers%2C+TJ&rft.au=Bond%2C+CS&rft.au=Peterson%2C+MR&rft.au=Hunter%2C+WN&rft.au=Fairlamb%2C+AH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3491871&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-67"><a href="#cite_ref-67">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCohenOosterbaanBerends1967" class="citation book cs1">Cohen JA, Oosterbaan RA, Berends F (1967). <a rel="nofollow" class="external text" href="https://web.archive.org/web/20180228070651/http://oai.dtic.mil/oai/oai">"[81] Organophosphorus compounds"</a>. Enzyme Structure. Methods in Enzymology. Vol. 11. pp. 686–702. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0076-6879%2867%2911085-9">10.1016/S0076-6879(67)11085-9</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-181860-9" title="Special:BookSources/978-0-12-181860-9"><bdi>978-0-12-181860-9</bdi></a>. Archived from <a rel="nofollow" class="external text" href="https://oai.dtic.mil/oai/oai">the original</a> on 28 February 2018.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=%5B81%5D+Organophosphorus+compounds&rft.btitle=Enzyme+Structure&rft.series=Methods+in+Enzymology&rft.pages=%3Cspan+class%3D%22nowrap%22%3E686-%3C%2Fspan%3E702&rft.date=1967&rft_id=info%3Adoi%2F10.1016%2FS0076-6879%2867%2911085-9&rft.isbn=978-0-12-181860-9&rft.aulast=Cohen&rft.aufirst=JA&rft.au=Oosterbaan%2C+RA&rft.au=Berends%2C+F&rft_id=https%3A%2F%2Foai.dtic.mil%2Foai%2Foai&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-68"><a href="#cite_ref-68">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBrenner2000" class="citation book cs1">Brenner GM (2000). Pharmacology (1st ed.). Philadelphia, PA: W.B. Saunders. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-7216-7757-6" title="Special:BookSources/978-0-7216-7757-6"><bdi>978-0-7216-7757-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Pharmacology&rft.place=Philadelphia%2C+PA&rft.edition=1st&rft.pub=W.B.+Saunders&rft.date=2000&rft.isbn=978-0-7216-7757-6&rft.aulast=Brenner&rft.aufirst=GM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Walsh_1984-69"><a href="#cite_ref-Walsh_1984_69-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFWalsh1984" class="citation journal cs1">Walsh CT (1984). "Suicide substrates, mechanism-based enzyme inactivators: recent developments". Annual Review of Biochemistry. 53: 493–535. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev.bi.53.070184.002425">10.1146/annurev.bi.53.070184.002425</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/6433782">6433782</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Biochemistry&rft.atitle=Suicide+substrates%2C+mechanism-based+enzyme+inactivators%3A+recent+developments&rft.volume=53&rft.pages=%3Cspan+class%3D%22nowrap%22%3E493-%3C%2Fspan%3E535&rft.date=1984&rft_id=info%3Adoi%2F10.1146%2Fannurev.bi.53.070184.002425&rft_id=info%3Apmid%2F6433782&rft.aulast=Walsh&rft.aufirst=CT&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-70"><a href="#cite_ref-70">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSaravanamuthuVickersBondPeterson2004" class="citation journal cs1">Saravanamuthu A, Vickers TJ, Bond CS, Peterson MR, Hunter WN, Fairlamb AH (July 2004). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3491871">"Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: a template for drug design"</a>. The Journal of Biological Chemistry. 279 (28): 29493–29500. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M403187200">10.1074/jbc.M403187200</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3491871">3491871</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15102853">15102853</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Two+interacting+binding+sites+for+quinacrine+derivatives+in+the+active+site+of+trypanothione+reductase%3A+a+template+for+drug+design&rft.volume=279&rft.issue=28&rft.pages=%3Cspan+class%3D%22nowrap%22%3E29493-%3C%2Fspan%3E29500&rft.date=2004-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3491871%23id-name%3DPMC&rft_id=info%3Apmid%2F15102853&rft_id=info%3Adoi%2F10.1074%2Fjbc.M403187200&rft.aulast=Saravanamuthu&rft.aufirst=A&rft.au=Vickers%2C+TJ&rft.au=Bond%2C+CS&rft.au=Peterson%2C+MR&rft.au=Hunter%2C+WN&rft.au=Fairlamb%2C+AH&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3491871&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-71"><a href="#cite_ref-71">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPereiraAndradeValentãoAndrade2017" class="citation book cs1">Pereira DM, Andrade C, Valentão P, Andrade PB (October 2017). <a rel="nofollow" class="external text" href="https://application.wiley-vch.de/books/sample/3527342052_c01.pdf">"Natural products as enzyme inhibitors."</a> (PDF). Natural Products Targeting Clinically Relevant Enzymes (First ed.). Wiley-VCH Verlag GmbH & Co. KGaA. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-527-34205-1" title="Special:BookSources/978-3-527-34205-1"><bdi>978-3-527-34205-1</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20221205143202/https://application.wiley-vch.de/books/sample/3527342052_c01.pdf">Archived</a> (PDF) from the original on 5 December 2022. Retrieved 3 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Natural+products+as+enzyme+inhibitors.&rft.btitle=Natural+Products+Targeting+Clinically+Relevant+Enzymes&rft.edition=First&rft.pub=Wiley-VCH+Verlag+GmbH+%26+Co.+KGaA&rft.date=2017-10&rft.isbn=978-3-527-34205-1&rft.aulast=Pereira&rft.aufirst=DM&rft.au=Andrade%2C+C&rft.au=Valent%C3%A3o%2C+P&rft.au=Andrade%2C+PB&rft_id=https%3A%2F%2Fapplication.wiley-vch.de%2Fbooks%2Fsample%2F3527342052_c01.pdf&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Hiratake_2005-72"><a href="#cite_ref-Hiratake_2005_72-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHiratake2005" class="citation journal cs1">Hiratake J (2005). "Enzyme inhibitors as chemical tools to study enzyme catalysis: rational design, synthesis, and applications". Chemical Record. 5 (4). New York, N.Y.: 209–28. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Ftcr.20045">10.1002/tcr.20045</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16041744">16041744</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Record&rft.atitle=Enzyme+inhibitors+as+chemical+tools+to+study+enzyme+catalysis%3A+rational+design%2C+synthesis%2C+and+applications&rft.volume=5&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E209-%3C%2Fspan%3E28&rft.date=2005&rft_id=info%3Adoi%2F10.1002%2Ftcr.20045&rft_id=info%3Apmid%2F16041744&rft.aulast=Hiratake&rft.aufirst=J&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-73"><a href="#cite_ref-73">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPagePitchford2021" class="citation book cs1">Page C, Pitchford S (2021). <a rel="nofollow" class="external text" href="https://www.clinicalkey.com/#!/content/book/3-s2.0-B9780702078187000352">"Venoms, toxins, poisons and herbs"</a>. Dale's Pharmacology Condensed E-Book (Third ed.). Philadelphia, Pa.: Elsevier Health Sciences. pp. 153–155. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-7020-7819-4" title="Special:BookSources/978-0-7020-7819-4"><bdi>978-0-7020-7819-4</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20130425174959/https://www.clinicalkey.com/#!/content/book/3-s2.0-B9780702078187000352">Archived</a> from the original on 25 April 2013. Retrieved 3 June 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Venoms%2C+toxins%2C+poisons+and+herbs&rft.btitle=Dale%27s+Pharmacology+Condensed+E-Book&rft.place=Philadelphia%2C+Pa.&rft.pages=%3Cspan+class%3D%22nowrap%22%3E153-%3C%2Fspan%3E155&rft.edition=Third&rft.pub=Elsevier+Health+Sciences&rft.date=2021&rft.isbn=978-0-7020-7819-4&rft.aulast=Page&rft.aufirst=C&rft.au=Pitchford%2C+S&rft_id=https%3A%2F%2Fwww.clinicalkey.com%2F%23%21%2Fcontent%2Fbook%2F3-s2.0-B9780702078187000352&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-74"><a href="#cite_ref-74">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFStenersen2004" class="citation book cs1">Stenersen J (2004). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=WjReuSXxl4YC&pg=PA82">"Chapter 5: Specific Enzyme Inhibitors"</a>. Chemical Pesticides Mode of Action and Toxicology. Boca Raton: CRC Press. pp. 73–114. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-203-64683-0" title="Special:BookSources/978-0-203-64683-0"><bdi>978-0-203-64683-0</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328005931/https://books.google.com/books?id=WjReuSXxl4YC&pg=PA82">Archived</a> from the original on 28 March 2023. Retrieved 14 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+5%3A+Specific+Enzyme+Inhibitors&rft.btitle=Chemical+Pesticides+Mode+of+Action+and+Toxicology&rft.place=Boca+Raton&rft.pages=%3Cspan+class%3D%22nowrap%22%3E73-%3C%2Fspan%3E114&rft.pub=CRC+Press&rft.date=2004&rft.isbn=978-0-203-64683-0&rft.aulast=Stenersen&rft.aufirst=J&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DWjReuSXxl4YC%26pg%3DPA82&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-75"><a href="#cite_ref-75">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGreathouseZahraBrady2021" class="citation book cs1">Greathouse B, Zahra F, Brady MF (September 2021). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK535428/">"Acetylcholinesterase Inhibitors Toxicity"</a>. StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30571049">30571049</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230117033429/https://www.ncbi.nlm.nih.gov/books/NBK535428/">Archived</a> from the original on 17 January 2023. Retrieved 14 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Acetylcholinesterase+Inhibitors+Toxicity&rft.btitle=StatPearls+%5BInternet%5D&rft.place=Treasure+Island+%28FL%29&rft.pub=StatPearls+Publishing&rft.date=2021-09&rft_id=info%3Apmid%2F30571049&rft.aulast=Greathouse&rft.aufirst=B&rft.au=Zahra%2C+F&rft.au=Brady%2C+MF&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK535428%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Orencio-Trejo_2010-76"><a href="#cite_ref-Orencio-Trejo_2010_76-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFOrencio-TrejoUtrillaFernández-SandovalHuerta-Beristain2010" class="citation book cs1">Orencio-Trejo M, Utrilla J, Fernández-Sandoval MT, Huerta-Beristain G, Gosset G, Martinez A (2010). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=TMhreJSpuU8C&pg=PA77">"Engineering the Escherichia coli Fermentative Metabolism"</a>. In Cordes M, Wittmann C, Krull R (eds.). Biosystems Engineering II: Linking Cellular Networks and Bioprocesses. Berlin: Springer Science & Business Media. pp. 77–78. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-642-13865-2" title="Special:BookSources/978-3-642-13865-2"><bdi>978-3-642-13865-2</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Engineering+the+Escherichia+coli+Fermentative+Metabolism&rft.btitle=Biosystems+Engineering+II%3A+Linking+Cellular+Networks+and+Bioprocesses&rft.place=Berlin&rft.pages=%3Cspan+class%3D%22nowrap%22%3E77-%3C%2Fspan%3E78&rft.pub=Springer+Science+%26+Business+Media&rft.date=2010&rft.isbn=978-3-642-13865-2&rft.aulast=Orencio-Trejo&rft.aufirst=M&rft.au=Utrilla%2C+J&rft.au=Fern%C3%A1ndez-Sandoval%2C+MT&rft.au=Huerta-Beristain%2C+G&rft.au=Gosset%2C+G&rft.au=Martinez%2C+A&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DTMhreJSpuU8C%26pg%3DPA77&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-77"><a href="#cite_ref-77">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFOkarLange1999" class="citation journal cs1">Okar DA, Lange AJ (1999). "Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes". BioFactors. 10 (1): 1–14. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fbiof.5520100101">10.1002/biof.5520100101</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10475585">10475585</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:24586866">24586866</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=BioFactors&rft.atitle=Fructose-2%2C6-bisphosphate+and+control+of+carbohydrate+metabolism+in+eukaryotes&rft.volume=10&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1-%3C%2Fspan%3E14&rft.date=1999&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A24586866%23id-name%3DS2CID&rft_id=info%3Apmid%2F10475585&rft_id=info%3Adoi%2F10.1002%2Fbiof.5520100101&rft.aulast=Okar&rft.aufirst=DA&rft.au=Lange%2C+AJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-78"><a href="#cite_ref-78">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPriceStevens1999" class="citation book cs1">Price NC, Stevens L (1999). Fundamentals of enzymology : the cell and molecular biology of catalytic proteins (3rd ed.). Oxford University Press. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-19-850229-6" title="Special:BookSources/978-0-19-850229-6"><bdi>978-0-19-850229-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Fundamentals+of+enzymology+%3A+the+cell+and+molecular+biology+of+catalytic+proteins&rft.edition=3rd&rft.pub=Oxford+University+Press&rft.date=1999&rft.isbn=978-0-19-850229-6&rft.aulast=Price&rft.aufirst=NC&rft.au=Stevens%2C+L&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-79"><a href="#cite_ref-79">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSmyth2004" class="citation journal cs1">Smyth TP (August 2004). <a rel="nofollow" class="external text" href="https://zenodo.org/record/998967">"Substrate variants versus transition state analogues as noncovalent reversible enzyme inhibitors"</a>. Bioorganic & Medicinal Chemistry. 12 (15): 4081–4088. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bmc.2004.05.041">10.1016/j.bmc.2004.05.041</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15246086">15246086</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328005934/https://zenodo.org/record/998967">Archived</a> from the original on 28 March 2023. Retrieved 14 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Bioorganic+%26+Medicinal+Chemistry&rft.atitle=Substrate+variants+versus+transition+state+analogues+as+noncovalent+reversible+enzyme+inhibitors&rft.volume=12&rft.issue=15&rft.pages=%3Cspan+class%3D%22nowrap%22%3E4081-%3C%2Fspan%3E4088&rft.date=2004-08&rft_id=info%3Adoi%2F10.1016%2Fj.bmc.2004.05.041&rft_id=info%3Apmid%2F15246086&rft.aulast=Smyth&rft.aufirst=TP&rft_id=https%3A%2F%2Fzenodo.org%2Frecord%2F998967&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-80"><a href="#cite_ref-80">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHartley1989" class="citation journal cs1">Hartley RW (November 1989). "Barnase and barstar: two small proteins to fold and fit together". Trends in Biochemical Sciences. 14 (11): 450–454. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0968-0004%2889%2990104-7">10.1016/0968-0004(89)90104-7</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2696173">2696173</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Biochemical+Sciences&rft.atitle=Barnase+and+barstar%3A+two+small+proteins+to+fold+and+fit+together&rft.volume=14&rft.issue=11&rft.pages=%3Cspan+class%3D%22nowrap%22%3E450-%3C%2Fspan%3E454&rft.date=1989-11&rft_id=info%3Adoi%2F10.1016%2F0968-0004%2889%2990104-7&rft_id=info%3Apmid%2F2696173&rft.aulast=Hartley&rft.aufirst=RW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-81"><a href="#cite_ref-81">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMaheshwari2022" class="citation book cs1">Maheshwari VL (2022). Natural Products as Enzyme Inhibitors. Singapore: Springer. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-981-19-0932-0" title="Special:BookSources/978-981-19-0932-0"><bdi>978-981-19-0932-0</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Natural+Products+as+Enzyme+Inhibitors&rft.place=Singapore&rft.pub=Springer&rft.date=2022&rft.isbn=978-981-19-0932-0&rft.aulast=Maheshwari&rft.aufirst=VL&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-82"><a href="#cite_ref-82">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBirk2003" class="citation book cs1">Birk Y (2003). Plant Protease Inhibitors: Significance in Nutrition, Plant Protection, Cancer Prevention and Genetic Engineering. Berlin: Springer. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-540-00118-8" title="Special:BookSources/978-3-540-00118-8"><bdi>978-3-540-00118-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Plant+Protease+Inhibitors%3A+Significance+in+Nutrition%2C+Plant+Protection%2C+Cancer+Prevention+and+Genetic+Engineering&rft.place=Berlin&rft.pub=Springer&rft.date=2003&rft.isbn=978-3-540-00118-8&rft.aulast=Birk&rft.aufirst=Y&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-83"><a href="#cite_ref-83">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTanGyllenhaalSoejarto2006" class="citation journal cs1">Tan G, Gyllenhaal C, Soejarto DD (March 2006). "Biodiversity as a source of anticancer drugs". Current Drug Targets. 7 (3): 265–277. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F138945006776054942">10.2174/138945006776054942</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16515527">16515527</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Drug+Targets&rft.atitle=Biodiversity+as+a+source+of+anticancer+drugs&rft.volume=7&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E265-%3C%2Fspan%3E277&rft.date=2006-03&rft_id=info%3Adoi%2F10.2174%2F138945006776054942&rft_id=info%3Apmid%2F16515527&rft.aulast=Tan&rft.aufirst=G&rft.au=Gyllenhaal%2C+C&rft.au=Soejarto%2C+DD&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-84"><a href="#cite_ref-84">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFAbalAndreuBarasoain2003" class="citation journal cs1">Abal M, Andreu JM, Barasoain I (June 2003). "Taxanes: microtubule and centrosome targets, and cell cycle dependent mechanisms of action". Current Cancer Drug Targets. 3 (3): 193–203. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1568009033481967">10.2174/1568009033481967</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12769688">12769688</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Cancer+Drug+Targets&rft.atitle=Taxanes%3A+microtubule+and+centrosome+targets%2C+and+cell+cycle+dependent+mechanisms+of+action&rft.volume=3&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E193-%3C%2Fspan%3E203&rft.date=2003-06&rft_id=info%3Adoi%2F10.2174%2F1568009033481967&rft_id=info%3Apmid%2F12769688&rft.aulast=Abal&rft.aufirst=M&rft.au=Andreu%2C+JM&rft.au=Barasoain%2C+I&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Hostettmann_2006-85"><a href="#cite_ref-Hostettmann_2006_85-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHostettmannBorlozUrbainMarston2006" class="citation journal cs1">Hostettmann K, Borloz A, Urbain A, Marston A (2006). "Natural Product Inhibitors of Acetylcholinesterase". Current Organic Chemistry. 10 (8): 825–847. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F138527206776894410">10.2174/138527206776894410</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Organic+Chemistry&rft.atitle=Natural+Product+Inhibitors+of+Acetylcholinesterase&rft.volume=10&rft.issue=8&rft.pages=%3Cspan+class%3D%22nowrap%22%3E825-%3C%2Fspan%3E847&rft.date=2006&rft_id=info%3Adoi%2F10.2174%2F138527206776894410&rft.aulast=Hostettmann&rft.aufirst=K&rft.au=Borloz%2C+A&rft.au=Urbain%2C+A&rft.au=Marston%2C+A&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Knight_2018-86"><a href="#cite_ref-Knight_2018_86-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKnightKhondokerMagillStewart2018" class="citation journal cs1">Knight R, Khondoker M, Magill N, Stewart R, Landau S (2018). <a rel="nofollow" class="external text" href="https://doi.org/10.1159%2F000486546">"A Systematic Review and Meta-Analysis of the Effectiveness of Acetylcholinesterase Inhibitors and Memantine in Treating the Cognitive Symptoms of Dementia"</a>. Dementia and Geriatric Cognitive Disorders. 45 (3–4): 131–151. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1159%2F000486546">10.1159/000486546</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29734182">29734182</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:13701908">13701908</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Dementia+and+Geriatric+Cognitive+Disorders&rft.atitle=A+Systematic+Review+and+Meta-Analysis+of+the+Effectiveness+of+Acetylcholinesterase+Inhibitors+and+Memantine+in+Treating+the+Cognitive+Symptoms+of+Dementia&rft.volume=45&rft.issue=%3Cspan+class%3D%22nowrap%22%3E3%E2%80%93%3C%2Fspan%3E4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E131-%3C%2Fspan%3E151&rft.date=2018&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A13701908%23id-name%3DS2CID&rft_id=info%3Apmid%2F29734182&rft_id=info%3Adoi%2F10.1159%2F000486546&rft.aulast=Knight&rft.aufirst=R&rft.au=Khondoker%2C+M&rft.au=Magill%2C+N&rft.au=Stewart%2C+R&rft.au=Landau%2C+S&rft_id=https%3A%2F%2Fdoi.org%2F10.1159%252F000486546&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-87"><a href="#cite_ref-87">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDeFratesHoehnsSakornbutGlascock2005" class="citation journal cs1">DeFrates LJ, Hoehns JD, Sakornbut EL, Glascock DG, Tew AR (January 2005). "Antimuscarinic intoxication resulting from the ingestion of moonflower seeds". The Annals of Pharmacotherapy. 39 (1): 173–176. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1345%2Faph.1D536">10.1345/aph.1D536</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15572604">15572604</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:36465515">36465515</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Annals+of+Pharmacotherapy&rft.atitle=Antimuscarinic+intoxication+resulting+from+the+ingestion+of+moonflower+seeds&rft.volume=39&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E173-%3C%2Fspan%3E176&rft.date=2005-01&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A36465515%23id-name%3DS2CID&rft_id=info%3Apmid%2F15572604&rft_id=info%3Adoi%2F10.1345%2Faph.1D536&rft.aulast=DeFrates&rft.aufirst=LJ&rft.au=Hoehns%2C+JD&rft.au=Sakornbut%2C+EL&rft.au=Glascock%2C+DG&rft.au=Tew%2C+AR&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-88"><a href="#cite_ref-88">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFVetter1998" class="citation journal cs1">Vetter J (January 1998). "Toxins of Amanita phalloides". Toxicon. 36 (1): 13–24. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1998Txcn...36...13V">1998Txcn...36...13V</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0041-0101%2897%2900074-3">10.1016/S0041-0101(97)00074-3</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9604278">9604278</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Toxicon&rft.atitle=Toxins+of+Amanita+phalloides&rft.volume=36&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E13-%3C%2Fspan%3E24&rft.date=1998-01&rft_id=info%3Apmid%2F9604278&rft_id=info%3Adoi%2F10.1016%2FS0041-0101%2897%2900074-3&rft_id=info%3Abibcode%2F1998Txcn...36...13V&rft.aulast=Vetter&rft.aufirst=J&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-89"><a href="#cite_ref-89">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHolmesMaynesPerreaultDawson2002" class="citation journal cs1">Holmes CF, Maynes JT, Perreault KR, Dawson JF, James MN (November 2002). "Molecular enzymology underlying regulation of protein phosphatase-1 by natural toxins". Current Medicinal Chemistry. 9 (22): 1981–1989. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F0929867023368827">10.2174/0929867023368827</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12369866">12369866</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Medicinal+Chemistry&rft.atitle=Molecular+enzymology+underlying+regulation+of+protein+phosphatase-1+by+natural+toxins&rft.volume=9&rft.issue=22&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1981-%3C%2Fspan%3E1989&rft.date=2002-11&rft_id=info%3Adoi%2F10.2174%2F0929867023368827&rft_id=info%3Apmid%2F12369866&rft.aulast=Holmes&rft.aufirst=CF&rft.au=Maynes%2C+JT&rft.au=Perreault%2C+KR&rft.au=Dawson%2C+JF&rft.au=James%2C+MN&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-90"><a href="#cite_ref-90">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBischoff2001" class="citation journal cs1">Bischoff K (October 2001). "The toxicology of microcystin-LR: occurrence, toxicokinetics, toxicodynamics, diagnosis and treatment". Veterinary and Human Toxicology. 43 (5): 294–297. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11577938">11577938</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Veterinary+and+Human+Toxicology&rft.atitle=The+toxicology+of+microcystin-LR%3A+occurrence%2C+toxicokinetics%2C+toxicodynamics%2C+diagnosis+and+treatment&rft.volume=43&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E294-%3C%2Fspan%3E297&rft.date=2001-10&rft_id=info%3Apmid%2F11577938&rft.aulast=Bischoff&rft.aufirst=K&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-91"><a href="#cite_ref-91">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSavageMorrison2003" class="citation book cs1">Savage GP, Morrison SC (2003). "Trypsin inhibitors.". In Caballero B (ed.). Encyclopedia of Food Sciences and Nutrition (Second ed.). Academic Press. pp. 5878–5884. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FB0-12-227055-X%2F00934-2">10.1016/B0-12-227055-X/00934-2</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-227055-0" title="Special:BookSources/978-0-12-227055-0"><bdi>978-0-12-227055-0</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Trypsin+inhibitors.&rft.btitle=Encyclopedia+of+Food+Sciences+and+Nutrition&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5878-%3C%2Fspan%3E5884&rft.edition=Second&rft.pub=Academic+Press&rft.date=2003&rft_id=info%3Adoi%2F10.1016%2FB0-12-227055-X%2F00934-2&rft.isbn=978-0-12-227055-0&rft.aulast=Savage&rft.aufirst=GP&rft.au=Morrison%2C+SC&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Polito_2019-92"><a href="#cite_ref-Polito_2019_92-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPolitoBortolottiBattelliCalafato2019" class="citation journal cs1">Polito L, Bortolotti M, Battelli MG, Calafato G, Bolognesi A (June 2019). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6628454">"Ricin: An Ancient Story for a Timeless Plant Toxin"</a>. Toxins. 11 (6): 324. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3390%2Ftoxins11060324">10.3390/toxins11060324</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6628454">6628454</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/31174319">31174319</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Toxins&rft.atitle=Ricin%3A+An+Ancient+Story+for+a+Timeless+Plant+Toxin&rft.volume=11&rft.issue=6&rft.pages=324&rft.date=2019-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6628454%23id-name%3DPMC&rft_id=info%3Apmid%2F31174319&rft_id=info%3Adoi%2F10.3390%2Ftoxins11060324&rft.aulast=Polito&rft.aufirst=L&rft.au=Bortolotti%2C+M&rft.au=Battelli%2C+MG&rft.au=Calafato%2C+G&rft.au=Bolognesi%2C+A&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6628454&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Sowa-Rogozińska_2019-93"><a href="#cite_ref-Sowa-Rogozińska_2019_93-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSowa-RogozińskaSominkaNowakowska-GołackaSandvig2019" class="citation journal cs1">Sowa-Rogozińska N, Sominka H, Nowakowska-Gołacka J, Sandvig K, Słomińska-Wojewódzka M (June 2019). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6628406">"Intracellular Transport and Cytotoxicity of the Protein Toxin Ricin"</a>. Toxins. 11 (6): 350. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3390%2Ftoxins11060350">10.3390/toxins11060350</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6628406">6628406</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/31216687">31216687</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Toxins&rft.atitle=Intracellular+Transport+and+Cytotoxicity+of+the+Protein+Toxin+Ricin&rft.volume=11&rft.issue=6&rft.pages=350&rft.date=2019-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6628406%23id-name%3DPMC&rft_id=info%3Apmid%2F31216687&rft_id=info%3Adoi%2F10.3390%2Ftoxins11060350&rft.aulast=Sowa-Rogozi%C5%84ska&rft.aufirst=N&rft.au=Sominka%2C+H&rft.au=Nowakowska-Go%C5%82acka%2C+J&rft.au=Sandvig%2C+K&rft.au=S%C5%82omi%C5%84ska-Wojew%C3%B3dzka%2C+M&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6628406&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-94"><a href="#cite_ref-94">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHartleyLord2004" class="citation journal cs1">Hartley MR, Lord JM (September 2004). "Cytotoxic ribosome-inactivating lectins from plants". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1701 (1–2): 1–14. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbapap.2004.06.004">10.1016/j.bbapap.2004.06.004</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15450171">15450171</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Proteins+and+Proteomics&rft.atitle=Cytotoxic+ribosome-inactivating+lectins+from+plants&rft.volume=1701&rft.issue=%3Cspan+class%3D%22nowrap%22%3E1%E2%80%93%3C%2Fspan%3E2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1-%3C%2Fspan%3E14&rft.date=2004-09&rft_id=info%3Adoi%2F10.1016%2Fj.bbapap.2004.06.004&rft_id=info%3Apmid%2F15450171&rft.aulast=Hartley&rft.aufirst=MR&rft.au=Lord%2C+JM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Finkel_2009-95">^ <a href="#cite_ref-Finkel_2009_95-0">a</a> <a href="#cite_ref-Finkel_2009_95-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFinkelCubedduClark2009" class="citation book cs1">Finkel R, Cubeddu LX, Clark MA (2009). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=Q4hG2gRhy7oC&pg=PA502">"Chapter 41: Antiinfammatory Drugs"</a>. Pharmacology (4th ed.). Philadelphia: Lippincott Williams & Wilkins. pp. 499–518 (502). <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-7817-7155-9" title="Special:BookSources/978-0-7817-7155-9"><bdi>978-0-7817-7155-9</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328005952/https://books.google.com/books?id=Q4hG2gRhy7oC&pg=PA502">Archived</a> from the original on 28 March 2023. Retrieved 14 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+41%3A+Antiinfammatory+Drugs&rft.btitle=Pharmacology&rft.place=Philadelphia&rft.pages=499-518+%28502%29&rft.edition=4th&rft.pub=Lippincott+Williams+%26+Wilkins&rft.date=2009&rft.isbn=978-0-7817-7155-9&rft.aulast=Finkel&rft.aufirst=R&rft.au=Cubeddu%2C+LX&rft.au=Clark%2C+MA&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DQ4hG2gRhy7oC%26pg%3DPA502&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Santos_2017-96">^ <a href="#cite_ref-Santos_2017_96-0">a</a> <a href="#cite_ref-Santos_2017_96-1">b</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSantosUrsuGaultonBento2017" class="citation journal cs1">Santos R, Ursu O, Gaulton A, Bento AP, Donadi RS, Bologa CG, et al. (January 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6314433">"A comprehensive map of molecular drug targets"</a>. Nature Reviews. Drug Discovery. 16 (1): 19–34 (Figure 1C). <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnrd.2016.230">10.1038/nrd.2016.230</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6314433">6314433</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/27910877">27910877</a>. <q>Figure 1C: Clinical success of privileged protein family classes (% approved drugs targeting each target class): Reductase 7.62, Kinase 5.94, Protease 3.35, Hydrolase 2.76, NPTase 2.09, Transferase 1.92, Lyase 1.59, Isomerase 1.51, Phosphodiesterase 1.50, Cytochrome p450 0.84, Epigenetic eraser 0.33, Total enzyme targets of approved drugs = 29.45%</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Reviews.+Drug+Discovery&rft.atitle=A+comprehensive+map+of+molecular+drug+targets&rft.volume=16&rft.issue=1&rft.pages=19-34+%28Figure+1C%29&rft.date=2017-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6314433%23id-name%3DPMC&rft_id=info%3Apmid%2F27910877&rft_id=info%3Adoi%2F10.1038%2Fnrd.2016.230&rft.aulast=Santos&rft.aufirst=R&rft.au=Ursu%2C+O&rft.au=Gaulton%2C+A&rft.au=Bento%2C+AP&rft.au=Donadi%2C+RS&rft.au=Bologa%2C+CG&rft.au=Karlsson%2C+A&rft.au=Al-Lazikani%2C+B&rft.au=Hersey%2C+A&rft.au=Oprea%2C+TI&rft.au=Overington%2C+JP&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6314433&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Kannaiyan_2018-97"><a href="#cite_ref-Kannaiyan_2018_97-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKannaiyanMahadevan2018" class="citation journal cs1">Kannaiyan R, Mahadevan D (December 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6322661">"A comprehensive review of protein kinase inhibitors for cancer therapy"</a>. Expert Review of Anticancer Therapy. 18 (12): 1249–1270. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F14737140.2018.1527688">10.1080/14737140.2018.1527688</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6322661">6322661</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30259761">30259761</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Expert+Review+of+Anticancer+Therapy&rft.atitle=A+comprehensive+review+of+protein+kinase+inhibitors+for+cancer+therapy&rft.volume=18&rft.issue=12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1249-%3C%2Fspan%3E1270&rft.date=2018-12&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6322661%23id-name%3DPMC&rft_id=info%3Apmid%2F30259761&rft_id=info%3Adoi%2F10.1080%2F14737140.2018.1527688&rft.aulast=Kannaiyan&rft.aufirst=R&rft.au=Mahadevan%2C+D&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6322661&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-McLornan_2021-98"><a href="#cite_ref-McLornan_2021_98-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMcLornanPopeGotlibHarrison2021" class="citation journal cs1">McLornan DP, Pope JE, Gotlib J, Harrison CN (August 2021). "Current and future status of JAK inhibitors". Lancet. 398 (10302): 803–816. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0140-6736%2821%2900438-4">10.1016/S0140-6736(21)00438-4</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/34454676">34454676</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:237311419">237311419</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Lancet&rft.atitle=Current+and+future+status+of+JAK+inhibitors&rft.volume=398&rft.issue=10302&rft.pages=%3Cspan+class%3D%22nowrap%22%3E803-%3C%2Fspan%3E816&rft.date=2021-08&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A237311419%23id-name%3DS2CID&rft_id=info%3Apmid%2F34454676&rft_id=info%3Adoi%2F10.1016%2FS0140-6736%2821%2900438-4&rft.aulast=McLornan&rft.aufirst=DP&rft.au=Pope%2C+JE&rft.au=Gotlib%2C+J&rft.au=Harrison%2C+CN&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-99"><a href="#cite_ref-99">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMcGuire2003" class="citation journal cs1">McGuire JJ (2003). "Anticancer antifolates: current status and future directions". Current Pharmaceutical Design. 9 (31): 2593–2613. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1381612033453712">10.2174/1381612033453712</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14529544">14529544</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Pharmaceutical+Design&rft.atitle=Anticancer+antifolates%3A+current+status+and+future+directions&rft.volume=9&rft.issue=31&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2593-%3C%2Fspan%3E2613&rft.date=2003&rft_id=info%3Adoi%2F10.2174%2F1381612033453712&rft_id=info%3Apmid%2F14529544&rft.aulast=McGuire&rft.aufirst=JJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-common_2019-100"><a href="#cite_ref-common_2019_100-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGoldsteinBurnettRosenPark2019" class="citation journal cs1">Goldstein I, Burnett AL, Rosen RC, Park PW, Stecher VJ (January 2019). "The Serendipitous Story of Sildenafil: An Unexpected Oral Therapy for Erectile Dysfunction". Sexual Medicine Reviews. 7 (1): 115–128. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.sxmr.2018.06.005">10.1016/j.sxmr.2018.06.005</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30301707">30301707</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:52945888">52945888</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Sexual+Medicine+Reviews&rft.atitle=The+Serendipitous+Story+of+Sildenafil%3A+An+Unexpected+Oral+Therapy+for+Erectile+Dysfunction&rft.volume=7&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E115-%3C%2Fspan%3E128&rft.date=2019-01&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A52945888%23id-name%3DS2CID&rft_id=info%3Apmid%2F30301707&rft_id=info%3Adoi%2F10.1016%2Fj.sxmr.2018.06.005&rft.aulast=Goldstein&rft.aufirst=I&rft.au=Burnett%2C+AL&rft.au=Rosen%2C+RC&rft.au=Park%2C+PW&rft.au=Stecher%2C+VJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-101"><a href="#cite_ref-101">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMaggiFilippiLeddaMagini2000" class="citation journal cs1">Maggi M, Filippi S, Ledda F, Magini A, Forti G (August 2000). <a rel="nofollow" class="external text" href="https://doi.org/10.1530%2Feje.0.1430143">"Erectile dysfunction: from biochemical pharmacology to advances in medical therapy"</a>. European Journal of Endocrinology. 143 (2): 143–154. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1530%2Feje.0.1430143">10.1530/eje.0.1430143</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10913932">10913932</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=European+Journal+of+Endocrinology&rft.atitle=Erectile+dysfunction%3A+from+biochemical+pharmacology+to+advances+in+medical+therapy&rft.volume=143&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E143-%3C%2Fspan%3E154&rft.date=2000-08&rft_id=info%3Adoi%2F10.1530%2Feje.0.1430143&rft_id=info%3Apmid%2F10913932&rft.aulast=Maggi&rft.aufirst=M&rft.au=Filippi%2C+S&rft.au=Ledda%2C+F&rft.au=Magini%2C+A&rft.au=Forti%2C+G&rft_id=https%3A%2F%2Fdoi.org%2F10.1530%252Feje.0.1430143&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Cochrane_2020-102"><a href="#cite_ref-Cochrane_2020_102-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCochraneLohans2020" class="citation journal cs1">Cochrane SA, Lohans CT (May 2020). <a rel="nofollow" class="external text" href="https://pure.qub.ac.uk/en/publications/breaking-down-the-cell-wall-strategies-for-antibiotic-discovery-targeting-bacterial-transpeptidases(e1bd1fbf-37a6-44ce-afdf-cc255bf217e6).html">"Breaking down the cell wall: Strategies for antibiotic discovery targeting bacterial transpeptidases"</a>. European Journal of Medicinal Chemistry. 194: 112262. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ejmech.2020.112262">10.1016/j.ejmech.2020.112262</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/32248005">32248005</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:214809706">214809706</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20230328005938/https://pure.qub.ac.uk/en/publications/breaking-down-the-cell-wall-strategies-for-antibiotic-discovery-t">Archived</a> from the original on 28 March 2023. Retrieved 20 July 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=European+Journal+of+Medicinal+Chemistry&rft.atitle=Breaking+down+the+cell+wall%3A+Strategies+for+antibiotic+discovery+targeting+bacterial+transpeptidases&rft.volume=194&rft.pages=112262&rft.date=2020-05&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A214809706%23id-name%3DS2CID&rft_id=info%3Apmid%2F32248005&rft_id=info%3Adoi%2F10.1016%2Fj.ejmech.2020.112262&rft.aulast=Cochrane&rft.aufirst=SA&rft.au=Lohans%2C+CT&rft_id=https%3A%2F%2Fpure.qub.ac.uk%2Fen%2Fpublications%2Fbreaking-down-the-cell-wall-strategies-for-antibiotic-discovery-targeting-bacterial-transpeptidases%28e1bd1fbf-37a6-44ce-afdf-cc255bf217e6%29.html&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Buynak_2007-103"><a href="#cite_ref-Buynak_2007_103-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFBuynak2007" class="citation journal cs1">Buynak JD (September 2007). "Cutting and stitching: the cross-linking of peptidoglycan in the assembly of the bacterial cell wall". ACS Chemical Biology. 2 (9): 602–5. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fcb700182u">10.1021/cb700182u</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17894443">17894443</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=ACS+Chemical+Biology&rft.atitle=Cutting+and+stitching%3A+the+cross-linking+of+peptidoglycan+in+the+assembly+of+the+bacterial+cell+wall&rft.volume=2&rft.issue=9&rft.pages=%3Cspan+class%3D%22nowrap%22%3E602-%3C%2Fspan%3E5&rft.date=2007-09&rft_id=info%3Adoi%2F10.1021%2Fcb700182u&rft_id=info%3Apmid%2F17894443&rft.aulast=Buynak&rft.aufirst=JD&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Dalhoff_2021-104"><a href="#cite_ref-Dalhoff_2021_104-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDalhoff2021" class="citation journal cs1">Dalhoff A (February 2021). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7851017">"Selective toxicity of antibacterial agents-still a valid concept or do we miss chances and ignore risks?"</a>. Infection. 49 (1): 29–56. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs15010-020-01536-y">10.1007/s15010-020-01536-y</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7851017">7851017</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33367978">33367978</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Infection&rft.atitle=Selective+toxicity+of+antibacterial+agents-still+a+valid+concept+or+do+we+miss+chances+and+ignore+risks%3F&rft.volume=49&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E29-%3C%2Fspan%3E56&rft.date=2021-02&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC7851017%23id-name%3DPMC&rft_id=info%3Apmid%2F33367978&rft_id=info%3Adoi%2F10.1007%2Fs15010-020-01536-y&rft.aulast=Dalhoff&rft.aufirst=A&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC7851017&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-105"><a href="#cite_ref-105">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFMobley2006" class="citation journal cs1">Mobley H (13 March 2006). <a rel="nofollow" class="external text" href="https://www.scientificamerican.com/article/how-do-antibiotics-kill-b/">"How do antibiotics kill bacterial cells but not human cells?"</a>. Scientific American. 294 (6): 98. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16711368">16711368</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220409085735/https://www.scientificamerican.com/article/how-do-antibiotics-kill-b/">Archived</a> from the original on 9 April 2022. Retrieved 9 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Scientific+American&rft.atitle=How+do+antibiotics+kill+bacterial+cells+but+not+human+cells%3F&rft.volume=294&rft.issue=6&rft.pages=98&rft.date=2006-03-13&rft_id=info%3Apmid%2F16711368&rft.aulast=Mobley&rft.aufirst=H&rft_id=https%3A%2F%2Fwww.scientificamerican.com%2Farticle%2Fhow-do-antibiotics-kill-b%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Zhang_2021-106"><a href="#cite_ref-Zhang_2021_106-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFZhangHeBaiRuan2021" class="citation journal cs1">Zhang L, He J, Bai L, Ruan S, Yang T, Luo Y (July 2021). "Ribosome-targeting antibacterial agents: Advances, challenges, and opportunities". Medicinal Research Reviews. 41 (4): 1855–1889. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fmed.21780">10.1002/med.21780</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33501747">33501747</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:231761270">231761270</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Medicinal+Research+Reviews&rft.atitle=Ribosome-targeting+antibacterial+agents%3A+Advances%2C+challenges%2C+and+opportunities&rft.volume=41&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1855-%3C%2Fspan%3E1889&rft.date=2021-07&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A231761270%23id-name%3DS2CID&rft_id=info%3Apmid%2F33501747&rft_id=info%3Adoi%2F10.1002%2Fmed.21780&rft.aulast=Zhang&rft.aufirst=L&rft.au=He%2C+J&rft.au=Bai%2C+L&rft.au=Ruan%2C+S&rft.au=Yang%2C+T&rft.au=Luo%2C+Y&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Yao_2017-107"><a href="#cite_ref-Yao_2017_107-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFYaoRock2017" class="citation journal cs1">Yao J, Rock CO (November 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364071">"Bacterial fatty acid metabolism in modern antibiotic discovery"</a>. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1862 (11): 1300–1309. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbalip.2016.09.014">10.1016/j.bbalip.2016.09.014</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364071">5364071</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/27668701">27668701</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Molecular+and+Cell+Biology+of+Lipids&rft.atitle=Bacterial+fatty+acid+metabolism+in+modern+antibiotic+discovery&rft.volume=1862&rft.issue=11&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1300-%3C%2Fspan%3E1309&rft.date=2017-11&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5364071%23id-name%3DPMC&rft_id=info%3Apmid%2F27668701&rft_id=info%3Adoi%2F10.1016%2Fj.bbalip.2016.09.014&rft.aulast=Yao&rft.aufirst=J&rft.au=Rock%2C+CO&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5364071&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-108"><a href="#cite_ref-108">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLiJingPanZhang2021" class="citation book cs1">Li G, Jing X, Pan, Zhang P, De Clercq E (2021). "Antiviral Classification". In Bamford D, Zuckerman MA (eds.). Encyclopedia of Virology. Vol. 5 (4th ed.). Amsterdam: Academic Press. pp. 129–130. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FB978-0-12-814515-9.00126-0">10.1016/B978-0-12-814515-9.00126-0</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-814516-6" title="Special:BookSources/978-0-12-814516-6"><bdi>978-0-12-814516-6</bdi></a>. <a href="/wiki/OCLC_(identifier)" class="mw-redirect" title="OCLC (identifier)">OCLC</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/oclc/1240584737">1240584737</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Antiviral+Classification&rft.btitle=Encyclopedia+of+Virology&rft.place=Amsterdam&rft.pages=%3Cspan+class%3D%22nowrap%22%3E129-%3C%2Fspan%3E130&rft.edition=4th&rft.pub=Academic+Press&rft.date=2021&rft_id=info%3Aoclcnum%2F1240584737&rft_id=info%3Adoi%2F10.1016%2FB978-0-12-814515-9.00126-0&rft.isbn=978-0-12-814516-6&rft.aulast=Li&rft.aufirst=G&rft.au=Jing%2C+X&rft.au=Pan&rft.au=Zhang%2C+P&rft.au=De+Clercq%2C+E&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Voshavar_2019-109"><a href="#cite_ref-Voshavar_2019_109-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFVoshavar2019" class="citation journal cs1">Voshavar C (2019). "Protease Inhibitors for the Treatment of HIV/AIDS: Recent Advances and Future Challenges". Current Topics in Medicinal Chemistry. 19 (18): 1571–1598. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1568026619666190619115243">10.2174/1568026619666190619115243</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/31237209">31237209</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:195356119">195356119</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Topics+in+Medicinal+Chemistry&rft.atitle=Protease+Inhibitors+for+the+Treatment+of+HIV%2FAIDS%3A+Recent+Advances+and+Future+Challenges&rft.volume=19&rft.issue=18&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1571-%3C%2Fspan%3E1598&rft.date=2019&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A195356119%23id-name%3DS2CID&rft_id=info%3Apmid%2F31237209&rft_id=info%3Adoi%2F10.2174%2F1568026619666190619115243&rft.aulast=Voshavar&rft.aufirst=C&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-de_Leuw_2018-110"><a href="#cite_ref-de_Leuw_2018_110-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFde_LeuwStephan2018" class="citation journal cs1">de Leuw P, Stephan C (April 2018). "Protease inhibitor therapy for hepatitis C virus-infection". Expert Opinion on Pharmacotherapy. 19 (6): 577–587. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1080%2F14656566.2018.1454428">10.1080/14656566.2018.1454428</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29595065">29595065</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4489039">4489039</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Expert+Opinion+on+Pharmacotherapy&rft.atitle=Protease+inhibitor+therapy+for+hepatitis+C+virus-infection&rft.volume=19&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E577-%3C%2Fspan%3E587&rft.date=2018-04&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A4489039%23id-name%3DS2CID&rft_id=info%3Apmid%2F29595065&rft_id=info%3Adoi%2F10.1080%2F14656566.2018.1454428&rft.aulast=de+Leuw&rft.aufirst=P&rft.au=Stephan%2C+C&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Li_2011-111"><a href="#cite_ref-Li_2011_111-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLiWangDe_Clercq2022" class="citation journal cs1">Li G, Wang Y, De Clercq E (April 2022). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9279714">"Approved HIV reverse transcriptase inhibitors in the past decade"</a>. Acta Pharmaceutica Sinica B. 12 (4): 1567–1590. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.apsb.2021.11.009">10.1016/j.apsb.2021.11.009</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9279714">9279714</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/35847492">35847492</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Acta+Pharmaceutica+Sinica+B&rft.atitle=Approved+HIV+reverse+transcriptase+inhibitors+in+the+past+decade&rft.volume=12&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1567-%3C%2Fspan%3E1590&rft.date=2022-04&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC9279714%23id-name%3DPMC&rft_id=info%3Apmid%2F35847492&rft_id=info%3Adoi%2F10.1016%2Fj.apsb.2021.11.009&rft.aulast=Li&rft.aufirst=G&rft.au=Wang%2C+Y&rft.au=De+Clercq%2C+E&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC9279714&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Gubareva_2022-112"><a href="#cite_ref-Gubareva_2022_112-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGubarevaMohan2022" class="citation journal cs1">Gubareva L, Mohan T (January 2022). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8725622">"Antivirals Targeting the Neuraminidase"</a>. Cold Spring Harbor Perspectives in Medicine. 12 (1): a038455. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1101%2Fcshperspect.a038455">10.1101/cshperspect.a038455</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8725622">8725622</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/32152244">32152244</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:212651676">212651676</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cold+Spring+Harbor+Perspectives+in+Medicine&rft.atitle=Antivirals+Targeting+the+Neuraminidase&rft.volume=12&rft.issue=1&rft.pages=a038455&rft.date=2022-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC8725622%23id-name%3DPMC&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A212651676%23id-name%3DS2CID&rft_id=info%3Apmid%2F32152244&rft_id=info%3Adoi%2F10.1101%2Fcshperspect.a038455&rft.aulast=Gubareva&rft.aufirst=L&rft.au=Mohan%2C+T&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC8725622&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Gentry_2019-113"><a href="#cite_ref-Gentry_2019_113-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGentryBognerDrach2019" class="citation journal cs1">Gentry BG, Bogner E, Drach JC (January 2019). "Targeting the terminase: An important step forward in the treatment and prophylaxis of human cytomegalovirus infections". Antiviral Research. 161: 116–124. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.antiviral.2018.11.005">10.1016/j.antiviral.2018.11.005</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/30472161">30472161</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:53763831">53763831</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Antiviral+Research&rft.atitle=Targeting+the+terminase%3A+An+important+step+forward+in+the+treatment+and+prophylaxis+of+human+cytomegalovirus+infections&rft.volume=161&rft.pages=%3Cspan+class%3D%22nowrap%22%3E116-%3C%2Fspan%3E124&rft.date=2019-01&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A53763831%23id-name%3DS2CID&rft_id=info%3Apmid%2F30472161&rft_id=info%3Adoi%2F10.1016%2Fj.antiviral.2018.11.005&rft.aulast=Gentry&rft.aufirst=BG&rft.au=Bogner%2C+E&rft.au=Drach%2C+JC&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-114"><a href="#cite_ref-114">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKuhrDorough1976" class="citation book cs1">Kuhr RJ, Dorough HW (1976). Carbamate Insecticides: Chemistry, Biochemistry, and Toxicology. Cleveland: CRC Press. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-87819-052-2" title="Special:BookSources/978-0-87819-052-2"><bdi>978-0-87819-052-2</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Carbamate+Insecticides%3A+Chemistry%2C+Biochemistry%2C+and+Toxicology&rft.place=Cleveland&rft.pub=CRC+Press&rft.date=1976&rft.isbn=978-0-87819-052-2&rft.aulast=Kuhr&rft.aufirst=RJ&rft.au=Dorough%2C+HW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-115"><a href="#cite_ref-115">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFStone2020" class="citation book cs1">Stone TW (October 2020). CNS Neurotransmitters and Neuromodulators: Acetylcholine (1st ed.). Boca Raton: CRC Press. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-00-009898-3" title="Special:BookSources/978-1-00-009898-3"><bdi>978-1-00-009898-3</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=CNS+Neurotransmitters+and+Neuromodulators%3A+Acetylcholine&rft.place=Boca+Raton&rft.edition=1st&rft.pub=CRC+Press&rft.date=2020-10&rft.isbn=978-1-00-009898-3&rft.aulast=Stone&rft.aufirst=TW&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Gupta_2006-116"><a href="#cite_ref-Gupta_2006_116-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGupta2006" class="citation book cs1">Gupta RC (2006). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=mFFoWG-x4rAC&q=Classification+and+Uses+of+Organophosphates+and+Carbamates&pg=PA5">"Classification and Uses of Organophosphates and Carbamates"</a>. In Gupta RC (ed.). Toxicology of Organophosphate and Carbamate Compounds. Amsterdam: Elsevier Academic Press. pp. 5–24. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-08-054310-9" title="Special:BookSources/978-0-08-054310-9"><bdi>978-0-08-054310-9</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220721073320/https://books.google.com/books?id=mFFoWG-x4rAC&q=Classification+and+Uses+of+Organophosphates+and+Carbamates&pg=PA5">Archived</a> from the original on 21 July 2022. Retrieved 21 July 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Classification+and+Uses+of+Organophosphates+and+Carbamates&rft.btitle=Toxicology+of+Organophosphate+and+Carbamate+Compounds&rft.place=Amsterdam&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5-%3C%2Fspan%3E24&rft.pub=Elsevier+Academic+Press&rft.date=2006&rft.isbn=978-0-08-054310-9&rft.aulast=Gupta&rft.aufirst=RC&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DmFFoWG-x4rAC%26q%3DClassification%2Band%2BUses%2Bof%2BOrganophosphates%2Band%2BCarbamates%26pg%3DPA5&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Farmakidis_2018-117"><a href="#cite_ref-Farmakidis_2018_117-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFFarmakidisPasnoorDimachkieBarohn2018" class="citation journal cs1">Farmakidis C, Pasnoor M, Dimachkie MM, Barohn RJ (May 2018). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6690491">"Treatment of Myasthenia Gravis"</a>. Neurologic Clinics. 36 (2): 311–337. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ncl.2018.01.011">10.1016/j.ncl.2018.01.011</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6690491">6690491</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29655452">29655452</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Neurologic+Clinics&rft.atitle=Treatment+of+Myasthenia+Gravis&rft.volume=36&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E311-%3C%2Fspan%3E337&rft.date=2018-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6690491%23id-name%3DPMC&rft_id=info%3Apmid%2F29655452&rft_id=info%3Adoi%2F10.1016%2Fj.ncl.2018.01.011&rft.aulast=Farmakidis&rft.aufirst=C&rft.au=Pasnoor%2C+M&rft.au=Dimachkie%2C+MM&rft.au=Barohn%2C+RJ&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC6690491&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-118"><a href="#cite_ref-118">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFButterworthIVMackeyWasnick2013" class="citation book cs1">Butterworth JF, IV, Mackey DC, Wasnick JD, eds. (2013). "Chapter 12. Cholinesterase Inhibitors & Other Pharmacologic Antagonists to Neuromuscular Blocking Agents.". <a rel="nofollow" class="external text" href="https://accessanesthesiology.mhmedical.com/content.aspx?bookid=564&sectionid=42800543">Morgan & Mikhail's Clinical Anesthesiology</a> (5th ed.). McGraw Hill. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220630044627/https://accessanesthesiology.mhmedical.com/content.aspx?bookid=564&sectionid=42800543">Archived</a> from the original on 30 June 2022. Retrieved 9 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+12.+Cholinesterase+Inhibitors+%26+Other+Pharmacologic+Antagonists+to+Neuromuscular+Blocking+Agents.&rft.btitle=Morgan+%26+Mikhail%27s+Clinical+Anesthesiology&rft.edition=5th&rft.pub=McGraw+Hill&rft.date=2013&rft_id=https%3A%2F%2Faccessanesthesiology.mhmedical.com%2Fcontent.aspx%3Fbookid%3D564%26sectionid%3D42800543&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Thapa_2017-119"><a href="#cite_ref-Thapa_2017_119-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFThapaLvXu2017" class="citation journal cs1">Thapa S, Lv M, Xu H (2017). "Acetylcholinesterase: A Primary Target for Drugs and Insecticides". Mini Reviews in Medicinal Chemistry. 17 (17): 1665–1676. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1389557517666170120153930">10.2174/1389557517666170120153930</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/28117022">28117022</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Mini+Reviews+in+Medicinal+Chemistry&rft.atitle=Acetylcholinesterase%3A+A+Primary+Target+for+Drugs+and+Insecticides&rft.volume=17&rft.issue=17&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1665-%3C%2Fspan%3E1676&rft.date=2017&rft_id=info%3Adoi%2F10.2174%2F1389557517666170120153930&rft_id=info%3Apmid%2F28117022&rft.aulast=Thapa&rft.aufirst=S&rft.au=Lv%2C+M&rft.au=Xu%2C+H&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-pmid16547651-120"><a href="#cite_ref-pmid16547651_120-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFTanEvansSingh2006" class="citation journal cs1">Tan S, Evans R, Singh B (March 2006). "Herbicidal inhibitors of amino acid biosynthesis and herbicide-tolerant crops". Amino Acids. 30 (2): 195–204. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2Fs00726-005-0254-1">10.1007/s00726-005-0254-1</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16547651">16547651</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:2358278">2358278</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Amino+Acids&rft.atitle=Herbicidal+inhibitors+of+amino+acid+biosynthesis+and+herbicide-tolerant+crops&rft.volume=30&rft.issue=2&rft.pages=%3Cspan+class%3D%22nowrap%22%3E195-%3C%2Fspan%3E204&rft.date=2006-03&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A2358278%23id-name%3DS2CID&rft_id=info%3Apmid%2F16547651&rft_id=info%3Adoi%2F10.1007%2Fs00726-005-0254-1&rft.aulast=Tan&rft.aufirst=S&rft.au=Evans%2C+R&rft.au=Singh%2C+B&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-121"><a href="#cite_ref-121">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFHiraiUchidaOhno2012" class="citation book cs1">Hirai K, Uchida A, Ohno R (2012). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=JSjzCAAAQBAJ&pg=PA180">"Major Synthetic Routes for Modern Herbicide Classes and Agrochemical Characteristics"</a>. In Böger P, Wakabayashi K, Hirai K (eds.). Herbicide Classes in Development. Springer Science & Business Media. pp. 179–195. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2F978-3-642-59416-8_10">10.1007/978-3-642-59416-8_10</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-642-59416-8" title="Special:BookSources/978-3-642-59416-8"><bdi>978-3-642-59416-8</bdi></a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220627073108/https://books.google.com/books?id=JSjzCAAAQBAJ&pg=PA180">Archived</a> from the original on 27 June 2022. Retrieved 27 June 2022. <q>Chapter 10.2.1: Sulfonylurea acetolactate synthase inhibitors</q></cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Major+Synthetic+Routes+for+Modern+Herbicide+Classes+and+Agrochemical+Characteristics&rft.btitle=Herbicide+Classes+in+Development&rft.pages=%3Cspan+class%3D%22nowrap%22%3E179-%3C%2Fspan%3E195&rft.pub=Springer+Science+%26+Business+Media&rft.date=2012&rft_id=info%3Adoi%2F10.1007%2F978-3-642-59416-8_10&rft.isbn=978-3-642-59416-8&rft.aulast=Hirai&rft.aufirst=K&rft.au=Uchida%2C+A&rft.au=Ohno%2C+R&rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3DJSjzCAAAQBAJ%26pg%3DPA180&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-122"><a href="#cite_ref-122">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFDuke1990" class="citation journal cs1">Duke SO (July 1990). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1567841">"Overview of herbicide mechanisms of action"</a>. Environmental Health Perspectives. 87: 263–271. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2307%2F3431034">10.2307/3431034</a>. <a href="/wiki/JSTOR_(identifier)" class="mw-redirect" title="JSTOR (identifier)">JSTOR</a> <a rel="nofollow" class="external text" href="https://www.jstor.org/stable/3431034">3431034</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1567841">1567841</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/1980104">1980104</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Environmental+Health+Perspectives&rft.atitle=Overview+of+herbicide+mechanisms+of+action&rft.volume=87&rft.pages=%3Cspan+class%3D%22nowrap%22%3E263-%3C%2Fspan%3E271&rft.date=1990-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1567841%23id-name%3DPMC&rft_id=info%3Apmid%2F1980104&rft_id=https%3A%2F%2Fwww.jstor.org%2Fstable%2F3431034%23id-name%3DJSTOR&rft_id=info%3Adoi%2F10.2307%2F3431034&rft.aulast=Duke&rft.aufirst=SO&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1567841&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-123"><a href="#cite_ref-123">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGangulyAlluri2021" class="citation book cs1">Ganguly AK, Alluri SS (12 September 2021). "Chapter 2: Enzyme Inhibitors". Medicinal Chemistry: A Look at How Drugs Are Discovered. Boca Raton, Florida: CRC Press. pp. 29–68. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-00-043721-8" title="Special:BookSources/978-1-00-043721-8"><bdi>978-1-00-043721-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+2%3A+Enzyme+Inhibitors&rft.btitle=Medicinal+Chemistry%3A+A+Look+at+How+Drugs+Are+Discovered&rft.place=Boca+Raton%2C+Florida&rft.pages=%3Cspan+class%3D%22nowrap%22%3E29-%3C%2Fspan%3E68&rft.pub=CRC+Press&rft.date=2021-09-12&rft.isbn=978-1-00-043721-8&rft.aulast=Ganguly&rft.aufirst=AK&rft.au=Alluri%2C+SS&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Rufer_2021-124"><a href="#cite_ref-Rufer_2021_124-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFRufer2021" class="citation journal cs1">Rufer AC (April 2021). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.drudis.2021.01.006">"Drug discovery for enzymes"</a>. Drug Discovery Today. 26 (4): 875–886. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.drudis.2021.01.006">10.1016/j.drudis.2021.01.006</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33454380">33454380</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:231633284">231633284</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Drug+Discovery+Today&rft.atitle=Drug+discovery+for+enzymes&rft.volume=26&rft.issue=4&rft.pages=%3Cspan+class%3D%22nowrap%22%3E875-%3C%2Fspan%3E886&rft.date=2021-04&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A231633284%23id-name%3DS2CID&rft_id=info%3Apmid%2F33454380&rft_id=info%3Adoi%2F10.1016%2Fj.drudis.2021.01.006&rft.aulast=Rufer&rft.aufirst=AC&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252Fj.drudis.2021.01.006&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-125"><a href="#cite_ref-125">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFLindquist2013" class="citation book cs1">Lindquist RN (October 2013). "The design of enzyme inhibitors: Transition state analogues.". In Ariëns EJ (ed.). Drug Design: Medicinal Chemistry: A Series of Monographs. Vol. 5. Elsevier. pp. 24–80.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=The+design+of+enzyme+inhibitors%3A+Transition+state+analogues.&rft.btitle=Drug+Design%3A+Medicinal+Chemistry%3A+A+Series+of+Monographs&rft.pages=%3Cspan+class%3D%22nowrap%22%3E24-%3C%2Fspan%3E80&rft.pub=Elsevier&rft.date=2013-10&rft.aulast=Lindquist&rft.aufirst=RN&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-126"><a href="#cite_ref-126">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFScapin2006" class="citation journal cs1">Scapin G (2006). "Structural biology and drug discovery". Current Pharmaceutical Design. 12 (17): 2087–2097. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F138161206777585201">10.2174/138161206777585201</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16796557">16796557</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Pharmaceutical+Design&rft.atitle=Structural+biology+and+drug+discovery&rft.volume=12&rft.issue=17&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2087-%3C%2Fspan%3E2097&rft.date=2006&rft_id=info%3Adoi%2F10.2174%2F138161206777585201&rft_id=info%3Apmid%2F16796557&rft.aulast=Scapin&rft.aufirst=G&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-127"><a href="#cite_ref-127">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFGohlkeKlebe2002" class="citation journal cs1">Gohlke H, Klebe G (August 2002). "Approaches to the description and prediction of the binding affinity of small-molecule ligands to macromolecular receptors". Angewandte Chemie. 41 (15): 2644–2676. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2F1521-3773%2820020802%2941%3A15%3C2644%3A%3AAID-ANIE2644%3E3.0.CO%3B2-O">10.1002/1521-3773(20020802)41:15<2644::AID-ANIE2644>3.0.CO;2-O</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12203463">12203463</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Angewandte+Chemie&rft.atitle=Approaches+to+the+description+and+prediction+of+the+binding+affinity+of+small-molecule+ligands+to+macromolecular+receptors&rft.volume=41&rft.issue=15&rft.pages=%3Cspan+class%3D%22nowrap%22%3E2644-%3C%2Fspan%3E2676&rft.date=2002-08&rft_id=info%3Adoi%2F10.1002%2F1521-3773%2820020802%2941%3A15%3C2644%3A%3AAID-ANIE2644%3E3.0.CO%3B2-O&rft_id=info%3Apmid%2F12203463&rft.aulast=Gohlke&rft.aufirst=H&rft.au=Klebe%2C+G&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-128"><a href="#cite_ref-128">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFKoppitzEis2006" class="citation journal cs1">Koppitz M, Eis K (June 2006). "Automated medicinal chemistry". Drug Discovery Today. 11 (11–12): 561–568. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.drudis.2006.04.005">10.1016/j.drudis.2006.04.005</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16713909">16713909</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Drug+Discovery+Today&rft.atitle=Automated+medicinal+chemistry&rft.volume=11&rft.issue=%3Cspan+class%3D%22nowrap%22%3E11%E2%80%93%3C%2Fspan%3E12&rft.pages=%3Cspan+class%3D%22nowrap%22%3E561-%3C%2Fspan%3E568&rft.date=2006-06&rft_id=info%3Adoi%2F10.1016%2Fj.drudis.2006.04.005&rft_id=info%3Apmid%2F16713909&rft.aulast=Koppitz&rft.aufirst=M&rft.au=Eis%2C+K&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Ciulli_2007-129"><a href="#cite_ref-Ciulli_2007_129-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFCiulliAbell2007" class="citation journal cs1">Ciulli A, Abell C (December 2007). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4441723">"Fragment-based approaches to enzyme inhibition"</a>. Current Opinion in Biotechnology. 18 (6): 489–96. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.copbio.2007.09.003">10.1016/j.copbio.2007.09.003</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4441723">4441723</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17959370">17959370</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Opinion+in+Biotechnology&rft.atitle=Fragment-based+approaches+to+enzyme+inhibition&rft.volume=18&rft.issue=6&rft.pages=%3Cspan+class%3D%22nowrap%22%3E489-%3C%2Fspan%3E96&rft.date=2007-12&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4441723%23id-name%3DPMC&rft_id=info%3Apmid%2F17959370&rft_id=info%3Adoi%2F10.1016%2Fj.copbio.2007.09.003&rft.aulast=Ciulli&rft.aufirst=A&rft.au=Abell%2C+C&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4441723&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Satz_2021-130"><a href="#cite_ref-Satz_2021_130-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFSatzKuaiPeng2021" class="citation journal cs1">Satz AL, Kuai L, Peng X (May 2021). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bmcl.2021.127851">"Selections and screenings of DNA-encoded chemical libraries against enzyme and cellular targets"</a>. Bioorganic & Medicinal Chemistry Letters. 39: 127851. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bmcl.2021.127851">10.1016/j.bmcl.2021.127851</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33631371">33631371</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:232059044">232059044</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Bioorganic+%26+Medicinal+Chemistry+Letters&rft.atitle=Selections+and+screenings+of+DNA-encoded+chemical+libraries+against+enzyme+and+cellular+targets&rft.volume=39&rft.pages=127851&rft.date=2021-05&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A232059044%23id-name%3DS2CID&rft_id=info%3Apmid%2F33631371&rft_id=info%3Adoi%2F10.1016%2Fj.bmcl.2021.127851&rft.aulast=Satz&rft.aufirst=AL&rft.au=Kuai%2C+L&rft.au=Peng%2C+X&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252Fj.bmcl.2021.127851&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-131"><a href="#cite_ref-131">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFPerezPenaFernandez-VegaScampavia2019" class="citation book cs1">Perez O, Pena J, Fernandez-Vega V, Scampavia L, Spicer T (2019). "Chapter 4: High Throughput Screening". Drug Discovery and Development. Boca Raton, Florida: CRC Press. pp. 47–69. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-315-11347-0" title="Special:BookSources/978-1-315-11347-0"><bdi>978-1-315-11347-0</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Chapter+4%3A+High+Throughput+Screening&rft.btitle=Drug+Discovery+and+Development&rft.place=Boca+Raton%2C+Florida&rft.pages=%3Cspan+class%3D%22nowrap%22%3E47-%3C%2Fspan%3E69&rft.pub=CRC+Press&rft.date=2019&rft.isbn=978-1-315-11347-0&rft.aulast=Perez&rft.aufirst=O&rft.au=Pena%2C+J&rft.au=Fernandez-Vega%2C+V&rft.au=Scampavia%2C+L&rft.au=Spicer%2C+T&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-Scarpino_2020-132"><a href="#cite_ref-Scarpino_2020_132-0">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFScarpinoFerenczyKeserű2020" class="citation journal cs1">Scarpino A, Ferenczy GG, Keserű GM (2020). "Covalent Docking in Drug Discovery: Scope and Limitations". Current Pharmaceutical Design. 26 (44): 5684–5699. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F1381612824999201105164942">10.2174/1381612824999201105164942</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33155894">33155894</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:226271153">226271153</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Pharmaceutical+Design&rft.atitle=Covalent+Docking+in+Drug+Discovery%3A+Scope+and+Limitations&rft.volume=26&rft.issue=44&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5684-%3C%2Fspan%3E5699&rft.date=2020&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A226271153%23id-name%3DS2CID&rft_id=info%3Apmid%2F33155894&rft_id=info%3Adoi%2F10.2174%2F1381612824999201105164942&rft.aulast=Scarpino&rft.aufirst=A&rft.au=Ferenczy%2C+GG&rft.au=Keser%C5%B1%2C+GM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> <li id="cite_note-133"><a href="#cite_ref-133">^</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite id="CITEREFElsässerGoettig2021" class="citation journal cs1">Elsässer B, Goettig P (March 2021). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8004986">"Mechanisms of Proteolytic Enzymes and Their Inhibition in QM/MM Studies"</a>. International Journal of Molecular Sciences. 22 (6): 3232. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.3390%2Fijms22063232">10.3390/ijms22063232</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8004986">8004986</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/33810118">33810118</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=International+Journal+of+Molecular+Sciences&rft.atitle=Mechanisms+of+Proteolytic+Enzymes+and+Their+Inhibition+in+QM%2FMM+Studies&rft.volume=22&rft.issue=6&rft.pages=3232&rft.date=2021-03&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC8004986%23id-name%3DPMC&rft_id=info%3Apmid%2F33810118&rft_id=info%3Adoi%2F10.3390%2Fijms22063232&rft.aulast=Els%C3%A4sser&rft.aufirst=B&rft.au=Goettig%2C+P&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC8004986&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2>[<a href="/w/index.php?title=Enzyme_inhibitor&action=edit&section=31" title="Edit section: External links">edit</a>]</div> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://www.brenda-enzymes.org">"BRENDA"</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20220401024216/https://www.brenda-enzymes.org/">Archived</a> from the original on 1 April 2022.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=BRENDA&rft_id=https%3A%2F%2Fwww.brenda-enzymes.org&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988">, Database of enzymes giving lists of known inhibitors for each entry</li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://pubchem.ncbi.nlm.nih.gov/">"PubChem"</a>. National Center for Biotechnology Information. National Library of Medicine.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=unknown&rft.jtitle=National+Center+for+Biotechnology+Information&rft.atitle=PubChem&rft_id=https%3A%2F%2Fpubchem.ncbi.nlm.nih.gov%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> Database of drugs and enzyme inhibitors</li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222" /><cite class="citation web cs1"><a rel="nofollow" class="external text" href="https://web.archive.org/web/20060620032006/http://www.chem.qmul.ac.uk/iubmb/kinetics/ek4t6.html#p6">"Symbolism and Terminology in Enzyme Kinetics"</a>. Archived from <a rel="nofollow" class="external text" href="https://iubmb.qmul.ac.uk/kinetics/ek4t6.html#p6">the original</a> on 20 June 2006.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=Symbolism+and+Terminology+in+Enzyme+Kinetics&rft_id=https%3A%2F%2Fiubmb.qmul.ac.uk%2Fkinetics%2Fek4t6.html%23p6&rfr_id=info%3Asid%2Fen.wikipedia.org%3AEnzyme+inhibitor" class="Z3988"> Recommendations of the Nomenclature Committee of the International Union of Biochemistry (NC-IUB) on enzyme inhibition terminology</li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol ul,.mw-parser-output .hlist ul dl,.mw-parser-output .hlist ul ol,.mw-parser-output .hlist ul ul{display:inline}.mw-parser-output .hlist .mw-empty-li{display:none}.mw-parser-output .hlist dt::after{content:": "}.mw-parser-output .hlist dd::after,.mw-parser-output .hlist li::after{content:" · ";font-weight:bold}.mw-parser-output .hlist dd:last-child::after,.mw-parser-output .hlist dt:last-child::after,.mw-parser-output .hlist li:last-child::after{content:none}.mw-parser-output .hlist dd dd:first-child::before,.mw-parser-output .hlist dd dt:first-child::before,.mw-parser-output .hlist dd li:first-child::before,.mw-parser-output .hlist dt dd:first-child::before,.mw-parser-output .hlist dt dt:first-child::before,.mw-parser-output .hlist dt li:first-child::before,.mw-parser-output .hlist li dd:first-child::before,.mw-parser-output .hlist li dt:first-child::before,.mw-parser-output .hlist li li:first-child::before{content:" (";font-weight:normal}.mw-parser-output .hlist dd dd:last-child::after,.mw-parser-output .hlist dd dt:last-child::after,.mw-parser-output .hlist dd li:last-child::after,.mw-parser-output .hlist dt dd:last-child::after,.mw-parser-output .hlist dt dt:last-child::after,.mw-parser-output .hlist dt li:last-child::after,.mw-parser-output .hlist li dd:last-child::after,.mw-parser-output .hlist li dt:last-child::after,.mw-parser-output .hlist li li:last-child::after{content:")";font-weight:normal}.mw-parser-output .hlist ol{counter-reset:listitem}.mw-parser-output .hlist ol>li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:" "counter(listitem)"\a0 "}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:" ("counter(listitem)"\a0 "}</style><style data-mw-deduplicate="TemplateStyles:r1236075235">.mw-parser-output .navbox{box-sizing:border-box;border:1px solid #a2a9b1;width:100%;clear:both;font-size:88%;text-align:center;padding:1px;margin:1em auto 0}.mw-parser-output .navbox .navbox{margin-top:0}.mw-parser-output .navbox+.navbox,.mw-parser-output .navbox+.navbox-styles+.navbox{margin-top:-1px}.mw-parser-output .navbox-inner,.mw-parser-output .navbox-subgroup{width:100%}.mw-parser-output .navbox-group,.mw-parser-output .navbox-title,.mw-parser-output .navbox-abovebelow{padding:0.25em 1em;line-height:1.5em;text-align:center}.mw-parser-output .navbox-group{white-space:nowrap;text-align:right}.mw-parser-output .navbox,.mw-parser-output .navbox-subgroup{background-color:#fdfdfd}.mw-parser-output .navbox-list{line-height:1.5em;border-color:#fdfdfd}.mw-parser-output .navbox-list-with-group{text-align:left;border-left-width:2px;border-left-style:solid}.mw-parser-output tr+tr>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Pharmacology:_enzyme_inhibition70" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><style data-mw-deduplicate="TemplateStyles:r1239400231">.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar ul{display:inline-block;white-space:nowrap;line-height:inherit}.mw-parser-output .navbar-brackets::before{margin-right:-0.125em;content:"[ "}.mw-parser-output .navbar-brackets::after{margin-left:-0.125em;content:" ]"}.mw-parser-output .navbar li{word-spacing:-0.125em}.mw-parser-output .navbar a>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}html.skin-theme-clientpref-night .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzyme_inhibition" title="Template:Enzyme inhibition"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzyme_inhibition" title="Template talk:Enzyme inhibition"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzyme_inhibition" title="Special:EditPage/Template:Enzyme inhibition"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Pharmacology:_enzyme_inhibition70" style="font-size:114%;margin:0 4em"><a href="/wiki/Pharmacology" title="Pharmacology">Pharmacology</a>: <a class="mw-selflink selflink">enzyme inhibition</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Class</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Competitive_inhibition" title="Competitive inhibition">Competitive inhibition</a></li> <li><a href="/wiki/Uncompetitive_inhibitor" class="mw-redirect" title="Uncompetitive inhibitor">Uncompetitive inhibition</a></li> <li><a href="/wiki/Non-competitive_inhibition" title="Non-competitive inhibition">Non-competitive inhibition</a></li> <li><a href="/wiki/Suicide_inhibition" title="Suicide inhibition">Suicide inhibition</a></li> <li><a href="/wiki/Mixed_inhibition" title="Mixed inhibition">Mixed inhibition</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Substrate</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductase</a> (EC 1)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>1.1 <a href="/wiki/Aldose_reductase_inhibitor" title="Aldose reductase inhibitor">Aldose reductase</a></li> <li><a href="/wiki/Statin" title="Statin">HMG-CoA reductase</a></li></ul> <ul><li>1.3 <a href="/wiki/5%CE%B1-Reductase_inhibitor" title="5α-Reductase inhibitor">5α-Reductase</a></li></ul> <ul><li>1.4 <a href="/wiki/Monoamine_oxidase_inhibitor" title="Monoamine oxidase inhibitor">Monoamine oxidase</a></li></ul> <ul><li>1.5 <a href="/wiki/Dihydrofolate_reductase_inhibitor" title="Dihydrofolate reductase inhibitor">Dihydrofolate reductase</a></li></ul> <ul><li>1.13 <a href="/wiki/Lipoxygenase_inhibitor" class="mw-redirect" title="Lipoxygenase inhibitor">Lipoxygenase</a></li></ul> <ul><li>1.14 <a href="/wiki/Aromatase_inhibitor" title="Aromatase inhibitor">Aromatase</a></li> <li><a href="/wiki/COX-2_inhibitor" class="mw-redirect" title="COX-2 inhibitor">COX-2</a></li></ul> <ul><li>1.17 <a href="/wiki/Xanthine_oxidase_inhibitor" title="Xanthine oxidase inhibitor">Xanthine oxidase</a></li> <li><a href="/wiki/Ribonucleotide_reductase_inhibitor" title="Ribonucleotide reductase inhibitor">Ribonucleotide reductase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Transferase" title="Transferase">Transferase</a> (EC 2)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>2.1 <a href="/wiki/COMT_inhibitor" class="mw-redirect" title="COMT inhibitor">COMT</a></li> <li><a href="/wiki/Thymidylate_synthase_inhibitor" title="Thymidylate synthase inhibitor">Thymidylate synthase</a></li></ul> <ul><li>2.4 <a href="/wiki/PARP_inhibitor" title="PARP inhibitor">PARP</a></li></ul> <ul><li>2.5 <a href="/wiki/Dihydropteroate_synthase_inhibitor" title="Dihydropteroate synthase inhibitor">Dihydropteroate synthetase</a></li> <li><a href="/wiki/Farnesyltransferase_inhibitor" title="Farnesyltransferase inhibitor">Farnesyltransferase</a></li></ul> <ul><li>2.6 <a href="/wiki/GABA_transaminase_inhibitor" title="GABA transaminase inhibitor">GABA transaminase</a></li></ul> <ul><li>2.7 <a href="/wiki/Nucleotidyltransferase" title="Nucleotidyltransferase">Nucleotidyltransferase</a> <ul><li><a href="/wiki/Integrase_inhibitor" title="Integrase inhibitor">Integrase</a></li> <li><a href="/wiki/Reverse-transcriptase_inhibitor" title="Reverse-transcriptase inhibitor">Reverse transcriptase</a></li></ul></li> <li><a href="/wiki/Protein_kinase_inhibitor" title="Protein kinase inhibitor">Protein kinase</a> <ul><li><a href="/wiki/Tyrosine_kinase_inhibitor" title="Tyrosine kinase inhibitor">Tyrosine kinase</a> <ul><li><a href="/wiki/Janus_kinase_inhibitor" title="Janus kinase inhibitor">Janus kinase</a></li></ul></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Hydrolase" title="Hydrolase">Hydrolase</a> (EC 3)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>3.1 <a href="/wiki/Phosphodiesterase_inhibitor" title="Phosphodiesterase inhibitor">Phosphodiesterase</a></li> <li><a href="/wiki/Acetylcholinesterase_inhibitor" title="Acetylcholinesterase inhibitor">Acetylcholinesterase</a></li> <li><a href="/wiki/Ribonuclease_inhibitor" title="Ribonuclease inhibitor">Ribonuclease</a></li></ul> <ul><li>3.2 <a href="/wiki/Polygalacturonase_inhibitor" title="Polygalacturonase inhibitor">Polygalacturonase</a></li> <li><a href="/wiki/Neuraminidase_inhibitor" title="Neuraminidase inhibitor">Neuraminidase</a></li> <li><a href="/wiki/Alpha-glucosidase_inhibitor" title="Alpha-glucosidase inhibitor">Alpha-glucosidase</a></li></ul> <ul><li>3.4 <a href="/wiki/Protease_inhibitor_(pharmacology)" title="Protease inhibitor (pharmacology)">Protease</a>: <a href="/wiki/Exopeptidase_inhibitor" title="Exopeptidase inhibitor">Exopeptidase</a> <ul><li><a href="/wiki/Dipeptidyl_peptidase-4_inhibitor" title="Dipeptidyl peptidase-4 inhibitor">DPP-4</a></li> <li><a href="/wiki/ACE_inhibitor" title="ACE inhibitor">ACE</a></li></ul></li> <li><a href="/wiki/Endopeptidase_inhibitor" title="Endopeptidase inhibitor">Endopeptidase</a> <ul><li><a href="/wiki/Trypsin_inhibitor" title="Trypsin inhibitor">Trypsin</a></li> <li><a href="/wiki/Renin_inhibitor" title="Renin inhibitor">Renin</a></li></ul></li> <li>Mixed <ul><li><a href="/wiki/Enkephalinase_inhibitor" title="Enkephalinase inhibitor">Enkephalinase</a></li> <li><a href="/wiki/Matrix_metalloproteinase_inhibitor" title="Matrix metalloproteinase inhibitor">Matrix metalloproteinase</a></li> <li><a href="/wiki/Oxytocinase_inhibitor" class="mw-redirect" title="Oxytocinase inhibitor">Oxytocinase</a></li></ul></li></ul> <ul><li>3.5 <a href="/wiki/Histone_deacetylase_inhibitor" title="Histone deacetylase inhibitor">Histone deacetylase</a></li> <li><a href="/wiki/Beta-lactamase_inhibitor" class="mw-redirect" title="Beta-lactamase inhibitor">Beta-lactamase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lyase" title="Lyase">Lyase</a> (EC 4)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>4.1 <a href="/wiki/Dopa_decarboxylase_inhibitor" class="mw-redirect" title="Dopa decarboxylase inhibitor">Dopa decarboxylase</a></li></ul> <ul><li>4.2 <a href="/wiki/Carbonic_anhydrase_inhibitor" title="Carbonic anhydrase inhibitor">Carbonic anhydrase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Miscellaneous</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Steroidogenesis_inhibitor" title="Steroidogenesis inhibitor">Steroidogenesis inhibitor</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235" /></div><div role="navigation" class="navbox" aria-labelledby="Topics_in_medicinal_chemistry33" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231" /><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Medicinal_chemistry" title="Template:Medicinal chemistry"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Medicinal_chemistry" title="Template talk:Medicinal chemistry"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Medicinal_chemistry" title="Special:EditPage/Template:Medicinal chemistry"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Topics_in_medicinal_chemistry33" style="font-size:114%;margin:0 4em">Topics in <a href="/wiki/Medicinal_chemistry" title="Medicinal chemistry">medicinal chemistry</a></div></th></tr><tr><td colspan="2" class="navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/ADME" title="ADME">ADME</a></li> <li><a href="/wiki/Bioavailability" title="Bioavailability">Bioavailability</a></li> <li><a href="/wiki/Chemogenomics" title="Chemogenomics">Chemogenomics</a></li> <li><a href="/wiki/Drug_class" title="Drug class">Drug class</a></li> <li><a href="/wiki/Drug_delivery" title="Drug delivery">Drug delivery</a></li> <li><a href="/wiki/Drug_design" title="Drug design">Drug design</a></li> <li><a href="/wiki/Drug_development" title="Drug development">Drug development</a></li> <li><a href="/wiki/Drug_discovery" title="Drug discovery">Drug discovery</a></li> <li><a href="/wiki/Targeted_drug_delivery" title="Targeted drug delivery">Drug targeting</a></li> <li><a class="mw-selflink selflink">Enzyme inhibitor</a></li> <li><a href="/wiki/Ligand_efficiency" title="Ligand efficiency">Ligand efficiency</a></li> <li><a href="/wiki/Lipinski%27s_rule_of_five" title="Lipinski's rule of five">Lipinski's rule of five</a></li> <li><a href="/wiki/Lipophilic_efficiency" title="Lipophilic efficiency">Lipophilic efficiency</a></li> <li><a href="/wiki/Mechanism_of_action" title="Mechanism of action">Mechanism of action</a></li> <li><a href="/wiki/Mode_of_action" title="Mode of action">Mode of action</a></li> <li><a href="/wiki/New_chemical_entity" title="New chemical entity">New chemical entity</a></li> <li><a href="/wiki/Pharmacodynamics" title="Pharmacodynamics">Pharmacodynamics</a></li> <li><a href="/wiki/Pharmacokinetics" title="Pharmacokinetics">Pharmacokinetics</a></li> <li><a href="/wiki/Pharmacology" title="Pharmacology">Pharmacology</a></li> <li><a href="/wiki/Pharmacophore" title="Pharmacophore">Pharmacophore</a></li> <li><a href="/wiki/Quantitative_structure%E2%80%93activity_relationship" title="Quantitative structure–activity relationship">Quantitative structure–activity relationship</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235" /></div><div role="navigation" class="navbox" aria-labelledby="Enzymes56" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231" /><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzymes" title="Template talk:Enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzymes" title="Special:EditPage/Template:Enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzymes56" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a class="mw-selflink selflink">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li>EC7 <a href="/wiki/Translocase" title="Translocase">Translocases</a> (<a href="/wiki/List_of_EC_numbers_(EC_7)" title="List of EC numbers (EC 7)">list</a>)</li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374" /><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235" /><style data-mw-deduplicate="TemplateStyles:r1038841319">.mw-parser-output .tooltip-dotted{border-bottom:1px dotted;cursor:help}</style></div><div role="navigation" class="navbox authority-control" aria-label="Navbox909" style="padding:3px"><table class="nowraplinks hlist navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Help:Authority_control" title="Help:Authority control">Authority control databases</a>: National <a href="https://www.wikidata.org/wiki/Q427492#identifiers" title="Edit this at Wikidata"><img alt="Edit this at Wikidata" src="//upload.wikimedia.org/wikipedia/en/thumb/8/8a/OOjs_UI_icon_edit-ltr-progressive.svg/10px-OOjs_UI_icon_edit-ltr-progressive.svg.png" decoding="async" width="10" height="10" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/8/8a/OOjs_UI_icon_edit-ltr-progressive.svg/15px-OOjs_UI_icon_edit-ltr-progressive.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/8/8a/OOjs_UI_icon_edit-ltr-progressive.svg/20px-OOjs_UI_icon_edit-ltr-progressive.svg.png 2x" data-file-width="20" data-file-height="20" /></a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"><ul><li><a rel="nofollow" class="external text" href="https://aleph.nkp.cz/F/?func=find-c&local_base=aut&ccl_term=ica=ph250749&CON_LNG=ENG">Czech Republic</a></li><li><a rel="nofollow" class="external text" href="https://datos.bne.es/resource/XX538926">Spain</a></li><li><a rel="nofollow" class="external text" href="https://kopkatalogs.lv/F?func=direct&local_base=lnc10&doc_number=000139242&P_CON_LNG=ENG">Latvia</a></li><li><a rel="nofollow" class="external text" href="https://www.nli.org.il/en/authorities/987007550782205171">Israel</a></li></ul></div></td></tr></tbody></table></div>    </div><noscript><img src="https://login.wikimedia.org/wiki/Special:CentralAutoLogin/start?useformat=desktop&type=1x1&usesul3=0" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div class="printfooter" data-nosnippet="">Retrieved from "<a dir="ltr" href="https://en.wikipedia.org/w/index.php?title=Enzyme_inhibitor&oldid=1246407205">https://en.wikipedia.org/w/index.php?title=Enzyme_inhibitor&oldid=1246407205</a>"</div></div> <div id="catlinks" class="catlinks" data-mw="interface"><div id="mw-normal-catlinks" class="mw-normal-catlinks"><a href="/wiki/Help:Category" title="Help:Category">Categories</a>: <ul><li><a href="/wiki/Category:Biochemical_reactions" title="Category:Biochemical reactions">Biochemical reactions</a></li><li><a href="/wiki/Category:Medicinal_chemistry" title="Category:Medicinal chemistry">Medicinal chemistry</a></li><li><a href="/wiki/Category:Metabolism" title="Category:Metabolism">Metabolism</a></li><li><a href="/wiki/Category:Enzyme_inhibitors" title="Category:Enzyme inhibitors">Enzyme inhibitors</a></li></ul></div><div id="mw-hidden-catlinks" class="mw-hidden-catlinks mw-hidden-cats-hidden">Hidden categories: <ul><li><a href="/wiki/Category:Articles_with_short_description" title="Category:Articles with short description">Articles with short description</a></li><li><a href="/wiki/Category:Short_description_is_different_from_Wikidata" title="Category:Short description is different from Wikidata">Short description is different from Wikidata</a></li><li><a href="/wiki/Category:Wikipedia_indefinitely_move-protected_pages" title="Category:Wikipedia indefinitely move-protected pages">Wikipedia indefinitely move-protected pages</a></li><li><a href="/wiki/Category:Featured_articles" title="Category:Featured articles">Featured articles</a></li><li><a href="/wiki/Category:Use_dmy_dates_from_July_2022" title="Category:Use dmy dates from July 2022">Use dmy dates from July 2022</a></li><li><a href="/wiki/Category:Articles_containing_potentially_dated_statements_from_2017" title="Category:Articles containing potentially dated statements from 2017">Articles containing potentially dated statements from 2017</a></li><li><a href="/wiki/Category:All_articles_containing_potentially_dated_statements" title="Category:All articles containing potentially dated statements">All articles containing potentially dated statements</a></li><li><a href="/wiki/Category:Pages_that_use_a_deprecated_format_of_the_chem_tags" title="Category:Pages that use a deprecated format of the chem tags">Pages that use a deprecated format of the chem tags</a></li></ul></div></div> </div> </main> </div> <div class="mw-footer-container"> <footer id="footer" class="mw-footer" > <ul id="footer-info"> <li id="footer-info-lastmod"> This page was last edited on 18 September 2024, at 19:29 (UTC).</li> <li id="footer-info-copyright">Text is available under the <a href="/wiki/Wikipedia:Text_of_the_Creative_Commons_Attribution-ShareAlike_4.0_International_License" title="Wikipedia:Text of the Creative Commons Attribution-ShareAlike 4.0 International License">Creative Commons Attribution-ShareAlike 4.0 License</a>; additional terms may apply. By using this site, you agree to the <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Terms_of_Use" class="extiw" title="foundation:Special:MyLanguage/Policy:Terms of Use">Terms of Use</a> and <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy" class="extiw" title="foundation:Special:MyLanguage/Policy:Privacy policy">Privacy Policy</a>. Wikipedia® is a registered trademark of the <a rel="nofollow" class="external text" href="https://wikimediafoundation.org/">Wikimedia Foundation, Inc.</a>, a non-profit organization.</li> </ul> <ul id="footer-places"> <li id="footer-places-privacy"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy">Privacy policy</a></li> <li id="footer-places-about"><a href="/wiki/Wikipedia:About">About Wikipedia</a></li> <li id="footer-places-disclaimers"><a href="/wiki/Wikipedia:General_disclaimer">Disclaimers</a></li> <li id="footer-places-contact"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us">Contact Wikipedia</a></li> <li id="footer-places-wm-codeofconduct"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Universal_Code_of_Conduct">Code of Conduct</a></li> <li id="footer-places-developers"><a href="https://developer.wikimedia.org">Developers</a></li> <li id="footer-places-statslink"><a href="https://stats.wikimedia.org/#/en.wikipedia.org">Statistics</a></li> <li id="footer-places-cookiestatement"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Cookie_statement">Cookie statement</a></li> <li id="footer-places-mobileview"><a href="//en.m.wikipedia.org/w/index.php?title=Enzyme_inhibitor&mobileaction=toggle_view_mobile" class="noprint stopMobileRedirectToggle">Mobile view</a></li> </ul> <ul id="footer-icons" class="noprint"> <li id="footer-copyrightico"><a href="https://www.wikimedia.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><picture><source media="(min-width: 500px)" srcset="/static/images/footer/wikimedia-button.svg" width="84" height="29"><img src="/static/images/footer/wikimedia.svg" width="25" height="25" alt="Wikimedia Foundation" lang="en" loading="lazy"></picture></a></li> <li id="footer-poweredbyico"><a href="https://www.mediawiki.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><picture><source media="(min-width: 500px)" srcset="/w/resources/assets/poweredby_mediawiki.svg" width="88" height="31"><img src="/w/resources/assets/mediawiki_compact.svg" alt="Powered by MediaWiki" lang="en" width="25" height="25" loading="lazy"></picture></a></li> </ul> </footer> </div> </div> </div> <div class="vector-header-container vector-sticky-header-container"> <div id="vector-sticky-header" class="vector-sticky-header"> <div class="vector-sticky-header-start"> <div class="vector-sticky-header-icon-start vector-button-flush-left vector-button-flush-right" aria-hidden="true"> <button class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-sticky-header-search-toggle" tabindex="-1" data-event-name="ui.vector-sticky-search-form.icon"> Search </button> </div> <div role="search" class="vector-search-box-vue vector-search-box-show-thumbnail vector-search-box"> <div class="vector-typeahead-search-container"> <div class="cdx-typeahead-search cdx-typeahead-search--show-thumbnail"> <form action="/w/index.php" id="vector-sticky-search-form" class="cdx-search-input cdx-search-input--has-end-button"> <div class="cdx-search-input__input-wrapper" data-search-loc="header-moved"> <div class="cdx-text-input cdx-text-input--has-start-icon"> <input class="cdx-text-input__input" type="search" name="search" placeholder="Search Wikipedia"> </div> <input type="hidden" name="title" value="Special:Search"> </div> <button class="cdx-button cdx-search-input__end-button">Search</button> </form> </div> </div> </div> <div class="vector-sticky-header-context-bar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-sticky-header-toc" class="vector-dropdown mw-portlet mw-portlet-sticky-header-toc vector-sticky-header-toc vector-button-flush-left" > <input type="checkbox" id="vector-sticky-header-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-sticky-header-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-sticky-header-toc-label" for="vector-sticky-header-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" > Toggle the table of contents </label> <div class="vector-dropdown-content"> <div id="vector-sticky-header-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <div class="vector-sticky-header-context-bar-primary" aria-hidden="true" >Enzyme inhibitor</div> </div> </div> <div class="vector-sticky-header-end" aria-hidden="true"> <div class="vector-sticky-header-icons"> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-talk-sticky-header" tabindex="-1" data-event-name="talk-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-subject-sticky-header" tabindex="-1" data-event-name="subject-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-history-sticky-header" tabindex="-1" data-event-name="history-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only mw-watchlink" id="ca-watchstar-sticky-header" tabindex="-1" data-event-name="watch-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-edit-sticky-header" tabindex="-1" data-event-name="wikitext-edit-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-ve-edit-sticky-header" tabindex="-1" data-event-name="ve-edit-sticky-header"> </a> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only" id="ca-viewsource-sticky-header" tabindex="-1" data-event-name="ve-edit-protected-sticky-header"> </a> </div> <div class="vector-sticky-header-buttons"> <button class="cdx-button cdx-button--weight-quiet mw-interlanguage-selector" id="p-lang-btn-sticky-header" tabindex="-1" data-event-name="ui.dropdown-p-lang-btn-sticky-header"> 33 languages </button> <a href="#" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive" id="ca-addsection-sticky-header" tabindex="-1" data-event-name="addsection-sticky-header"> Add topic </a> </div> <div class="vector-sticky-header-icon-end"> <div class="vector-user-links"> </div> </div> </div> </div> </div> <div class="mw-portlet mw-portlet-dock-bottom emptyPortlet" id="p-dock-bottom"> <ul> </ul> </div> <script>(RLQ=window.RLQ||[]).push(function(){mw.config.set({"wgHostname":"mw-web.eqiad.main-5679484b6d-8765j","wgBackendResponseTime":318,"wgPageParseReport":{"limitreport":{"cputime":"1.259","walltime":"1.545","ppvisitednodes":{"value":13630,"limit":1000000},"postexpandincludesize":{"value":390094,"limit":2097152},"templateargumentsize":{"value":3541,"limit":2097152},"expansiondepth":{"value":16,"limit":100},"expensivefunctioncount":{"value":4,"limit":500},"unstrip-depth":{"value":1,"limit":20},"unstrip-size":{"value":573519,"limit":5000000},"entityaccesscount":{"value":1,"limit":400},"timingprofile":["100.00% 1193.247 1 -total"," 57.05% 680.760 1 Template:Reflist"," 28.77% 343.282 86 Template:Cite_journal"," 19.80% 236.237 46 Template:Cite_book"," 8.93% 106.586 23 Template:Rp"," 8.25% 98.420 23 Template:R/superscript"," 7.17% 85.615 4 Template:Navbox"," 7.11% 84.861 1 Template:Short_description"," 6.98% 83.340 1 Template:Enzyme_inhibition"," 4.55% 54.262 7 Template:Main_other"]},"scribunto":{"limitreport-timeusage":{"value":"0.736","limit":"10.000"},"limitreport-memusage":{"value":7075509,"limit":52428800}},"cachereport":{"origin":"mw-web.eqiad.main-65bf7dbd64-gv4m9","timestamp":"20250325194046","ttl":2592000,"transientcontent":false}}});});</script> <script type="application/ld+json">{"@context":"https:\/\/schema.org","@type":"Article","name":"Enzyme inhibitor","url":"https:\/\/en.wikipedia.org\/wiki\/Enzyme_inhibitor","sameAs":"http:\/\/www.wikidata.org\/entity\/Q427492","mainEntity":"http:\/\/www.wikidata.org\/entity\/Q427492","author":{"@type":"Organization","name":"Contributors to Wikimedia projects"},"publisher":{"@type":"Organization","name":"Wikimedia Foundation, Inc.","logo":{"@type":"ImageObject","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-hor-googpub.png"}},"datePublished":"2006-06-07T15:19:20Z","dateModified":"2024-09-18T19:29:20Z","image":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/d\/dd\/Enzyme_inhibitors_2.svg","headline":"molecule that binds to an enzyme and decreases its activity"}</script> </body> </html>