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<span class="vector-toc-numb">2</span> <span>Substrate specificity</span> </div> </a> <button aria-controls="toc-Substrate_specificity-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Substrate specificity subsection</span> </button> <ul id="toc-Substrate_specificity-sublist" class="vector-toc-list"> <li id="toc-Trypsin-like" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Trypsin-like"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Trypsin-like</span> </div> </a> <ul id="toc-Trypsin-like-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chymotrypsin-like" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chymotrypsin-like"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Chymotrypsin-like</span> </div> </a> <ul id="toc-Chymotrypsin-like-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Thrombin-like" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Thrombin-like"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Thrombin-like</span> </div> </a> <ul id="toc-Thrombin-like-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Elastase-like" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Elastase-like"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Elastase-like</span> </div> </a> <ul id="toc-Elastase-like-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Subtilisin-like" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Subtilisin-like"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.5</span> <span>Subtilisin-like</span> </div> </a> <ul id="toc-Subtilisin-like-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Catalytic_mechanism" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Catalytic_mechanism"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Catalytic mechanism</span> </div> </a> <button aria-controls="toc-Catalytic_mechanism-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Catalytic mechanism subsection</span> </button> <ul id="toc-Catalytic_mechanism-sublist" class="vector-toc-list"> <li id="toc-Additional_stabilizing_effects" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Additional_stabilizing_effects"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>Additional stabilizing effects</span> </div> </a> <ul id="toc-Additional_stabilizing_effects-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Regulation_of_serine_protease_activity" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Regulation_of_serine_protease_activity"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Regulation of serine protease activity</span> </div> </a> <button aria-controls="toc-Regulation_of_serine_protease_activity-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Regulation of serine protease activity subsection</span> </button> <ul id="toc-Regulation_of_serine_protease_activity-sublist" class="vector-toc-list"> <li id="toc-Zymogen_activation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Zymogen_activation"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Zymogen activation</span> </div> </a> <ul id="toc-Zymogen_activation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Inhibition" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Inhibition"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Inhibition</span> </div> </a> <ul id="toc-Inhibition-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Role_in_disease" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Role_in_disease"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Role in disease</span> </div> </a> <ul id="toc-Role_in_disease-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Diagnostic_use" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Diagnostic_use"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Diagnostic use</span> </div> </a> <ul id="toc-Diagnostic_use-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Antimicrobial_effect" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Antimicrobial_effect"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Antimicrobial effect</span> </div> </a> <ul id="toc-Antimicrobial_effect-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>See also</span> </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 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>References</span> </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 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>External links</span> </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" > <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" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span class="vector-dropdown-label-text">Toggle the table of contents</span> </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"><span class="mw-page-title-main">Serine protease</span></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 19 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-19" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">19 languages</span> </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/%D8%A8%D8%B1%D9%88%D8%AA%D9%8A%D9%8A%D8%B2_%D8%A7%D9%84%D8%B3%D9%8A%D8%B1%D9%8A%D9%86" title="بروتييز السيرين – Arabic" lang="ar" hreflang="ar" data-title="بروتييز السيرين" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Serin-proteaza" title="Serin-proteaza – Bosnian" lang="bs" hreflang="bs" data-title="Serin-proteaza" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Proteasa_serina" title="Proteasa serina – Catalan" lang="ca" hreflang="ca" data-title="Proteasa serina" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Serinproteasen" title="Serinproteasen – German" lang="de" hreflang="de" data-title="Serinproteasen" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Serina_proteasa" title="Serina proteasa – Spanish" lang="es" hreflang="es" data-title="Serina proteasa" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%B3%D8%B1%DB%8C%D9%86_%D9%BE%D8%B1%D9%88%D8%AA%D8%A6%D8%A7%D8%B2" title="سرین پروتئاز – Persian" lang="fa" hreflang="fa" data-title="سرین پروتئاز" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Prot%C3%A9ase_%C3%A0_s%C3%A9rine" title="Protéase à sérine – French" lang="fr" hreflang="fr" data-title="Protéase à sérine" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Serina_protease" title="Serina protease – Galician" lang="gl" hreflang="gl" data-title="Serina protease" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Serin_proteasi" title="Serin proteasi – Italian" lang="it" hreflang="it" data-title="Serin proteasi" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%A1%D7%A8%D7%99%D7%9F_%D7%A4%D7%A8%D7%95%D7%98%D7%90%D7%96" title="סרין פרוטאז – Hebrew" lang="he" hreflang="he" data-title="סרין פרוטאז" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Serineprotease" title="Serineprotease – Dutch" lang="nl" hreflang="nl" data-title="Serineprotease" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%BB%E3%83%AA%E3%83%B3%E3%83%97%E3%83%AD%E3%83%86%E3%82%A2%E3%83%BC%E3%82%BC" title="セリンプロテアーゼ – Japanese" lang="ja" hreflang="ja" data-title="セリンプロテアーゼ" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Proteazy_serynowe" title="Proteazy serynowe – Polish" lang="pl" hreflang="pl" data-title="Proteazy serynowe" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Serina_protease" title="Serina protease – Portuguese" lang="pt" hreflang="pt" data-title="Serina protease" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%A1%D0%B5%D1%80%D0%B8%D0%BD%D0%BE%D0%B2%D1%8B%D0%B5_%D0%BF%D1%80%D0%BE%D1%82%D0%B5%D0%B0%D0%B7%D1%8B" title="Сериновые протеазы – Russian" lang="ru" hreflang="ru" data-title="Сериновые протеазы" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Serinska_proteaza" title="Serinska proteaza – Serbian" lang="sr" hreflang="sr" data-title="Serinska proteaza" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Serinproteas" title="Serinproteas – Swedish" lang="sv" hreflang="sv" data-title="Serinproteas" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%A1%D0%B5%D1%80%D0%B8%D0%BD%D0%BE%D0%B2%D1%96_%D0%BF%D1%80%D0%BE%D1%82%D0%B5%D0%B0%D0%B7%D0%B8" title="Серинові протеази – Ukrainian" lang="uk" hreflang="uk" data-title="Серинові протеази" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target"><span>Українська</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E4%B8%9D%E6%B0%A8%E9%85%B8%E8%9B%8B%E7%99%BD%E9%85%B6" title="丝氨酸蛋白酶 – Chinese" lang="zh" hreflang="zh" data-title="丝氨酸蛋白酶" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q87324999#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></span></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 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data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"><span class="mw-redirectedfrom">(Redirected from <a href="/w/index.php?title=Serine_endopeptidase&redirect=no" class="mw-redirect" title="Serine endopeptidase">Serine endopeptidase</a>)</span></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">Class of enzymes</div> <style data-mw-deduplicate="TemplateStyles:r1257001546">.mw-parser-output .infobox-subbox{padding:0;border:none;margin:-3px;width:auto;min-width:100%;font-size:100%;clear:none;float:none;background-color:transparent}.mw-parser-output .infobox-3cols-child{margin:auto}.mw-parser-output .infobox .navbar{font-size:100%}@media screen{html.skin-theme-clientpref-night .mw-parser-output .infobox-full-data:not(.notheme)>div:not(.notheme)[style]{background:#1f1f23!important;color:#f8f9fa}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .infobox-full-data:not(.notheme) div:not(.notheme){background:#1f1f23!important;color:#f8f9fa}}@media(min-width:640px){body.skin--responsive .mw-parser-output .infobox-table{display:table!important}body.skin--responsive .mw-parser-output .infobox-table>caption{display:table-caption!important}body.skin--responsive .mw-parser-output .infobox-table>tbody{display:table-row-group}body.skin--responsive .mw-parser-output .infobox-table tr{display:table-row!important}body.skin--responsive .mw-parser-output .infobox-table th,body.skin--responsive .mw-parser-output .infobox-table td{padding-left:inherit;padding-right:inherit}}</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">Serine protease</th></tr><tr><td colspan="2" class="infobox-image"><span class="mw-default-size" typeof="mw:File/Frameless"><a href="/wiki/File:Chymotrypsin_enzyme.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/86/Chymotrypsin_enzyme.png/220px-Chymotrypsin_enzyme.png" decoding="async" width="220" height="149" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/86/Chymotrypsin_enzyme.png/330px-Chymotrypsin_enzyme.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/86/Chymotrypsin_enzyme.png/440px-Chymotrypsin_enzyme.png 2x" data-file-width="640" data-file-height="434" /></a></span><div class="infobox-caption">Crystal structure of bovine chymotrypsin. The catalytic residues are shown as yellow sticks. Rendered from PDB <a rel="nofollow" class="external text" href="http://www.rcsb.org/pdb/explore/explore.do?structureId=1CBW">1CBW</a>.</div></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Identifiers</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC no.</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.enzyme-database.org/query.php?ec=3.4.21.-">3.4.21.-</a></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Databases</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/IntEnz" title="IntEnz">IntEnz</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=3.4.21.-">IntEnz view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/BRENDA" title="BRENDA">BRENDA</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://www.brenda-enzymes.org/enzyme.php?ecno=3.4.21.-">BRENDA entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/ExPASy" class="mw-redirect" title="ExPASy">ExPASy</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/3.4.21.-">NiceZyme view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/KEGG" title="KEGG">KEGG</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.genome.jp/dbget-bin/www_bget?enzyme+3.4.21.-">KEGG entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/MetaCyc" title="MetaCyc">MetaCyc</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://biocyc.org/META/substring-search?type=NIL&object=3.4.21.-">metabolic pathway</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/PRIAM_enzyme-specific_profiles" title="PRIAM enzyme-specific profiles">PRIAM</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://priam.prabi.fr/cgi-bin/PRIAM_profiles_CurrentRelease.pl?EC=3.4.21.-">profile</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a> structures</th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity.rcsb_ec_lineage.id:3.4.21.-">RCSB PDB</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/search/index?ec_number:3.4.21.-">PDBe</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=3.4.21.-">PDBsum</a></td></tr><tr><td colspan="2" class="infobox-full-data" style="background-color: #eee"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1257001546"><table class="infobox mw-collapsible mw-collapsed" style="float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%"><tbody><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Search</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed_Central" title="PubMed Central">PMC</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=3.4.21.-%5BEC/RN%20Number%5D%20AND%20pubmed%20pmc%20local%5Bsb%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed" title="PubMed">PubMed</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=3.4.21.-%5BEC/RN%20Number%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">NCBI</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/protein?term=3.4.21.-%5BEC/RN%20Number%5D">proteins</a></td></tr></tbody></table></td></tr></tbody></table> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:1UTN.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/d/d5/1UTN.png/250px-1UTN.png" decoding="async" width="250" height="188" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/d5/1UTN.png/375px-1UTN.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/d5/1UTN.png/500px-1UTN.png 2x" data-file-width="640" data-file-height="480" /></a><figcaption><a href="/wiki/X-ray_crystallography" title="X-ray crystallography">Crystal structure</a> of <a href="/wiki/Trypsin" title="Trypsin">Trypsin</a>, a typical serine protease.</figcaption></figure> <p><b>Serine proteases</b> (or <b>serine endopeptidases</b>) are <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> that cleave <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a> in <a href="/wiki/Protein" title="Protein">proteins</a>. <a href="/wiki/Serine" title="Serine">Serine</a> serves as the <a href="/wiki/Nucleophilic" class="mw-redirect" title="Nucleophilic">nucleophilic</a> <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> at the (enzyme's) <a href="/wiki/Active_site" title="Active site">active site</a>.<sup id="cite_ref-Hedstrom2002_1-0" class="reference"><a href="#cite_note-Hedstrom2002-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> They are found ubiquitously in both <a href="/wiki/Eukaryotes" class="mw-redirect" title="Eukaryotes">eukaryotes</a> and <a href="/wiki/Prokaryotes" class="mw-redirect" title="Prokaryotes">prokaryotes</a>. Serine proteases fall into two broad categories based on their structure: <a href="/wiki/Chymotrypsin" title="Chymotrypsin">chymotrypsin</a>-like (trypsin-like) or <a href="/wiki/Subtilisin" title="Subtilisin">subtilisin</a>-like.<sup id="cite_ref-Madala2010_2-0" class="reference"><a href="#cite_note-Madala2010-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Classification">Classification</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=1" title="Edit section: Classification"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/MEROPS" title="MEROPS">MEROPS</a> protease classification system counts 16 <a href="/wiki/Protein_superfamily" title="Protein superfamily">superfamilies</a> (as of 2013) each containing many <a href="/wiki/Protein_family" title="Protein family">families</a>. Each superfamily uses the <a href="/wiki/Catalytic_triad" title="Catalytic triad">catalytic triad</a> or dyad in a different <a href="/wiki/Protein_fold" class="mw-redirect" title="Protein fold">protein fold</a> and so represent <a href="/wiki/Convergent_evolution" title="Convergent evolution">convergent evolution</a> of the <a href="/wiki/Catalytic_mechanism" class="mw-redirect" title="Catalytic mechanism">catalytic mechanism</a>. The majority belong to the S1 family of the <a href="/wiki/PA_clan" class="mw-redirect" title="PA clan">PA clan</a> (superfamily) of proteases. </p><p>For <a href="/wiki/Protein_superfamily" title="Protein superfamily">superfamilies</a>, P: superfamily, containing a mixture of <a href="/wiki/Nucleophile" title="Nucleophile">nucleophile</a> class families, S: purely serine proteases. superfamily. Within each superfamily, <a href="/wiki/Protein_family" title="Protein family">families</a> are designated by their catalytic nucleophile, (S: serine proteases). </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:2PTN.gif" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a2/2PTN.gif/220px-2PTN.gif" decoding="async" width="220" height="156" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a2/2PTN.gif/330px-2PTN.gif 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a2/2PTN.gif/440px-2PTN.gif 2x" data-file-width="1014" data-file-height="720" /></a><figcaption>Hinge motion in disordered activation domain in Trypsinogen (PDB ID: <a rel="nofollow" class="external text" href="https://www.rcsb.org/3d-view/2ptn">2PTN</a>). The hinges predicted using <a rel="nofollow" class="external text" href="https://github.com/Pranavkhade/PACKMAN">PACKMAN</a> Hinge prediction<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> are colored in blue (residues 23:28) and red (residues 175:182). The green colored region is the active site. Motion is generated using hdANM<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>.</figcaption></figure> <table class="wikitable"> <caption>Families of serine proteases </caption> <tbody><tr> <th><a href="/wiki/Protein_superfamily" title="Protein superfamily">Super-<br />family</a> </th> <th><a href="/wiki/Protein_family" title="Protein family">Families</a> </th> <th>Examples </th></tr> <tr> <td>SB</td> <td>S8, S53</td> <td><a href="/wiki/Subtilisin" title="Subtilisin">Subtilisin</a> (<i><a href="/wiki/Bacillus_licheniformis" title="Bacillus licheniformis">Bacillus licheniformis</a></i>) </td></tr> <tr> <td>SC</td> <td>S9, S10, S15, S28, S33, S37</td> <td><a href="/wiki/Prolyl_oligopeptidase" class="mw-redirect" title="Prolyl oligopeptidase">Prolyl oligopeptidase</a> (<i><a href="/wiki/Sus_scrofa" class="mw-redirect" title="Sus scrofa">Sus scrofa</a></i>) </td></tr> <tr> <td>SE</td> <td>S11, S12, S13</td> <td><a href="/w/index.php?title=D-Ala-D-Ala_peptidase_C&action=edit&redlink=1" class="new" title="D-Ala-D-Ala peptidase C (page does not exist)">D-Ala-D-Ala peptidase C</a> (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>SF</td> <td>S24, S26</td> <td><a href="/wiki/Signal_peptidase" title="Signal peptidase">Signal peptidase</a> I (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>SH</td> <td>S21, S73, S77, S78, S80</td> <td>Cytomegalovirus <a href="/wiki/Assemblin" title="Assemblin">assemblin</a> (human <a href="/wiki/Herpesvirus" class="mw-redirect" title="Herpesvirus">herpesvirus</a> 5) </td></tr> <tr> <td>SJ</td> <td>S16, S50, S69</td> <td><a href="/wiki/Lon-A_peptidase" class="mw-redirect" title="Lon-A peptidase">Lon-A peptidase</a> (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>SK</td> <td>S14, S41, S49</td> <td><a href="/wiki/ATP-dependent_Clp_protease_proteolytic_subunit" title="ATP-dependent Clp protease proteolytic subunit">Clp protease</a> (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>SO</td> <td>S74</td> <td>Phage K1F endosialidase CIMCD self-cleaving protein (Enterobacteria <a href="/w/index.php?title=Phage_K1F&action=edit&redlink=1" class="new" title="Phage K1F (page does not exist)">phage K1F</a>) </td></tr> <tr> <td>SP</td> <td>S59</td> <td><a href="/wiki/Nucleoporin" title="Nucleoporin">Nucleoporin</a> 145 (<i><a href="/wiki/Homo_sapiens" class="mw-redirect" title="Homo sapiens">Homo sapiens</a></i>) </td></tr> <tr> <td>SR</td> <td>S60</td> <td><a href="/wiki/Lactoferrin" title="Lactoferrin">Lactoferrin</a> (<i><a href="/wiki/Homo_sapiens" class="mw-redirect" title="Homo sapiens">Homo sapiens</a></i>) </td></tr> <tr> <td>SS</td> <td>S66</td> <td><a href="/w/index.php?title=Murein_tetrapeptidase_LD-carboxypeptidase&action=edit&redlink=1" class="new" title="Murein tetrapeptidase LD-carboxypeptidase (page does not exist)">Murein tetrapeptidase LD-carboxypeptidase</a> (<i><a href="/wiki/Pseudomonas_aeruginosa" title="Pseudomonas aeruginosa">Pseudomonas aeruginosa</a></i>) </td></tr> <tr> <td>ST</td> <td>S54</td> <td><a href="/wiki/Rhomboid_protease" title="Rhomboid protease">Rhomboid</a>-1 (<i><a href="/wiki/Drosophila_melanogaster" title="Drosophila melanogaster">Drosophila melanogaster</a></i>) </td></tr> <tr> <td><a href="/wiki/PA_clan" class="mw-redirect" title="PA clan">PA</a></td> <td>S1, S3, S6, S7, S29, S30, S31, S32, <br />S39, S46, S55, S64, S65, S75</td> <td><a href="/wiki/Chymotrypsin" title="Chymotrypsin">Chymotrypsin</a> A (<i><a href="/wiki/Bos_taurus" class="mw-redirect" title="Bos taurus">Bos taurus</a></i>) </td></tr> <tr> <td>PB</td> <td>S45, S63</td> <td><a href="/wiki/Penicillin_acylase" class="mw-redirect" title="Penicillin acylase">Penicillin G acylase</a> precursor (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>PC</td> <td>S51</td> <td><a href="/wiki/Dipeptidase_E" title="Dipeptidase E">Dipeptidase E</a> (<i><a href="/wiki/Escherichia_coli" title="Escherichia coli">Escherichia coli</a></i>) </td></tr> <tr> <td>PE</td> <td>P1</td> <td><a href="/w/index.php?title=DmpA_aminopeptidase&action=edit&redlink=1" class="new" title="DmpA aminopeptidase (page does not exist)">DmpA aminopeptidase</a> (<i><a href="/wiki/Brucella_anthropi" title="Brucella anthropi">Brucella anthropi</a></i>) </td></tr> <tr> <td data-sort-value="" style="background: var(--background-color-interactive, #ececec); color: var(--color-base, inherit); vertical-align: middle; text-align: center;" class="table-na">None</td> <td>S48, S62, S68, S71, S72, S79, S81</td> <td> </td></tr></tbody></table> <div class="mw-heading mw-heading2"><h2 id="Substrate_specificity">Substrate specificity</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=2" title="Edit section: Substrate specificity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Serine proteases are characterised by a distinctive structure, consisting of two beta-barrel domains that converge at the catalytic active site. These <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> can be further categorised based on their substrate specificity as either trypsin-like, chymotrypsin-like or elastase-like.<sup id="cite_ref-Ovaere2009_5-0" class="reference"><a href="#cite_note-Ovaere2009-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Trypsin-like">Trypsin-like</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=3" title="Edit section: Trypsin-like"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Trypsin-like proteases cleave peptide bonds following a positively charged amino acid (<a href="/wiki/Lysine" title="Lysine">lysine</a> or <a href="/wiki/Arginine" title="Arginine">arginine</a>).<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> This specificity is driven by the residue which lies at the base of the enzyme's S1 pocket (generally a negatively charged <a href="/wiki/Aspartic_acid" title="Aspartic acid">aspartic acid</a> or <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a>). </p> <div class="mw-heading mw-heading3"><h3 id="Chymotrypsin-like">Chymotrypsin-like</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=4" title="Edit section: Chymotrypsin-like"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The S1 pocket of chymotrypsin-like enzymes is more hydrophobic than in trypsin-like proteases. This results in a specificity for medium to large sized hydrophobic residues, such as <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>, <a href="/wiki/Phenylalanine" title="Phenylalanine">phenylalanine</a> and <a href="/wiki/Tryptophan" title="Tryptophan">tryptophan</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Thrombin-like">Thrombin-like</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=5" title="Edit section: Thrombin-like"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>These include <a href="/wiki/Thrombin" title="Thrombin">thrombin</a>, tissue activating plasminogen and <a href="/wiki/Plasmin" title="Plasmin">plasmin</a>. They have been found to have roles in coagulation and digestion as well as in the pathophysiology of neurodegenerative disorders such as Alzheimer's and Parkinson's induced dementia. Many highly-toxic thrombin-like serine protease isoforms are found in snake venoms.<sup id="cite_ref-:0_7-0" class="reference"><a href="#cite_note-:0-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Elastase-like">Elastase-like</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=6" title="Edit section: Elastase-like"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Elastase-like proteases have a much smaller S1 cleft than either trypsin- or chymotrypsin-like proteases. Consequently, residues such as <a href="/wiki/Alanine" title="Alanine">alanine</a>, <a href="/wiki/Glycine" title="Glycine">glycine</a> and <a href="/wiki/Valine" title="Valine">valine</a> tend to be preferred. </p> <div class="mw-heading mw-heading3"><h3 id="Subtilisin-like">Subtilisin-like</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=7" title="Edit section: Subtilisin-like"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Subtilisin" title="Subtilisin">Subtilisin</a> is a serine protease in <a href="/wiki/Prokaryotes" class="mw-redirect" title="Prokaryotes">prokaryotes</a>. Subtilisin is evolutionarily unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a <a href="/wiki/Catalytic_triad" title="Catalytic triad">catalytic triad</a>, to create a nucleophilic <a href="/wiki/Serine" title="Serine">serine</a>. This is the classic example used to illustrate <a href="/wiki/Convergent_evolution" title="Convergent evolution">convergent evolution</a>, since the same mechanism evolved twice independently during <a href="/wiki/Evolution" title="Evolution">evolution</a>. </p> <div class="mw-heading mw-heading2"><h2 id="Catalytic_mechanism">Catalytic mechanism</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=8" title="Edit section: Catalytic mechanism"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File"><a href="/wiki/File:Serine_protease_mechanism_by_snellios.png" class="mw-file-description" title="serine protease reaction mechanism"><img alt="serine protease reaction mechanism" src="//upload.wikimedia.org/wikipedia/commons/thumb/1/17/Serine_protease_mechanism_by_snellios.png/400px-Serine_protease_mechanism_by_snellios.png" decoding="async" width="400" height="355" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/17/Serine_protease_mechanism_by_snellios.png/600px-Serine_protease_mechanism_by_snellios.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/17/Serine_protease_mechanism_by_snellios.png/800px-Serine_protease_mechanism_by_snellios.png 2x" data-file-width="1002" data-file-height="889" /></a><figcaption>serine protease reaction mechanism</figcaption></figure> <p>The main player in the catalytic mechanism in the serine proteases is the catalytic triad. The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all <a href="/wiki/Protein_superfamily" title="Protein superfamily">superfamilies</a> of serine protease enzymes. The triad is a coordinated structure consisting of three <a href="/wiki/Amino_acids" class="mw-redirect" title="Amino acids">amino acids</a>: <a href="/wiki/Histidine" title="Histidine">His</a> 57, <a href="/wiki/Serine" title="Serine">Ser</a> 195 (hence the name "serine protease") and <a href="/wiki/Aspartic_acid" title="Aspartic acid">Asp</a> 102. These three key amino acids each play an essential role in the cleaving ability of the proteases. While the amino acid members of the triad are located far from one another on the sequence of the protein, due to folding, they will be very close to one another in the heart of the enzyme. The particular geometry of the triad members are highly characteristic to their specific function: it was shown that the position of just four points of the triad characterize the function of the containing enzyme.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p><p>In the event of catalysis, an ordered mechanism occurs in which several intermediates are generated. The catalysis of the peptide cleavage can be seen as a <a href="/wiki/Ping-pong" class="mw-redirect" title="Ping-pong">ping-pong</a> catalysis, in which a <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrate</a> binds (in this case, the polypeptide being cleaved), a product is released (the C-terminus "half" of the peptide with amino group visible), another substrate binds (in this case, water), and another product is released (the N-terminus "half" of the peptide with carboxyl group visible). </p><p>Each amino acid in the triad performs a specific task in this process: </p> <ul><li>The <a href="/wiki/Serine" title="Serine">serine</a> has an -OH group that is able to act as a <a href="/wiki/Nucleophile" title="Nucleophile">nucleophile</a>, attacking the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> carbon of the <a href="/wiki/Scissile_bond" title="Scissile bond">scissile</a> peptide bond of the substrate.</li> <li>A pair of electrons on the <a href="/wiki/Histidine" title="Histidine">histidine</a> nitrogen has the ability to accept the <a href="/wiki/Hydrogen" title="Hydrogen">hydrogen</a> from the <a href="/wiki/Serine" title="Serine">serine</a> -OH group, thus coordinating the attack of the <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bond</a>.</li> <li>The <a href="/wiki/Carboxyl" class="mw-redirect" title="Carboxyl">carboxyl</a> group on the <a href="/wiki/Aspartic_acid" title="Aspartic acid">aspartic acid</a> in turn <a href="/wiki/Hydrogen_bonds" class="mw-redirect" title="Hydrogen bonds">hydrogen bonds</a> with the <a href="/wiki/Histidine" title="Histidine">histidine</a>, making the nitrogen atom mentioned above much more <a href="/wiki/Electronegative" class="mw-redirect" title="Electronegative">electronegative</a>.</li></ul> <p>The whole reaction can be summarized as follows: </p> <ul><li>The <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptide</a> substrate binds to the surface of the serine protease enzyme such that the scissile bond is inserted into the active site of the enzyme, with the carbonyl carbon of this bond positioned near the <a href="/wiki/Nucleophilic" class="mw-redirect" title="Nucleophilic">nucleophilic</a> <a href="/wiki/Serine" title="Serine">serine</a>.</li> <li>The <a href="/wiki/Serine" title="Serine">serine</a> -OH attacks the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> carbon, and the nitrogen of the <a href="/wiki/Histidine" title="Histidine">histidine</a> accepts the hydrogen from the -OH of the [serine] and a pair of electrons from the double bond of the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> oxygen moves to the oxygen. As a result, a tetrahedral intermediate is generated.</li> <li>The bond joining the nitrogen and the carbon in the peptide bond is now broken. The covalent electrons creating this bond move to attack the hydrogen of the <a href="/wiki/Histidine" title="Histidine">histidine</a>, breaking the connection. The electrons that previously moved from the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> oxygen double bond move back from the negative oxygen to recreate the bond, generating an acyl-enzyme intermediate.</li> <li>Now, water comes into the reaction. Water replaces the <a href="/wiki/N-terminus" title="N-terminus">N-terminus</a> of the cleaved peptide, and attacks the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> carbon. Once again, the electrons from the double bond move to the oxygen making it negative, as the bond between the oxygen of the water and the carbon is formed. This is coordinated by the nitrogen of the <a href="/wiki/Histidine" title="Histidine">histidine</a>, which accepts a proton from the water. Overall, this generates another tetrahedral intermediate.</li> <li>In a final reaction, the bond formed in the first step between the <a href="/wiki/Serine" title="Serine">serine</a> and the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> carbon moves to attack the hydrogen that the <a href="/wiki/Histidine" title="Histidine">histidine</a> just acquired. The now electron-deficient <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> carbon re-forms the double bond with the oxygen. As a result, the <a href="/wiki/C-terminus" title="C-terminus">C-terminus</a> of the peptide is now ejected.</li></ul> <div class="mw-heading mw-heading3"><h3 id="Additional_stabilizing_effects">Additional stabilizing effects</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=9" title="Edit section: Additional stabilizing effects"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>It was discovered that additional amino acids of the protease, <i>Gly 193</i> and <i>Ser 195</i>, are involved in creating what is called an <i><a href="/wiki/Oxyanion" title="Oxyanion">oxyanion</a> hole</i>. Both <i>Gly 193</i> and <i>Ser 195</i> can donate backbone hydrogens for hydrogen bonding. When the <a href="/wiki/Tetrahedral_intermediate" class="mw-redirect" title="Tetrahedral intermediate">tetrahedral intermediate</a> of step 1 and step 3 are generated, the negative oxygen ion, having accepted the electrons from the <a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">carbonyl</a> double bond, fits perfectly into the oxyanion hole. In effect, serine proteases preferentially bind the <a href="/wiki/Transition_state" title="Transition state">transition state</a> and the overall structure is favored, lowering the <a href="/wiki/Activation_energy" title="Activation energy">activation energy</a> of the reaction. This "preferential binding" is responsible for much of the catalytic efficiency of the enzyme. </p> <div class="mw-heading mw-heading2"><h2 id="Regulation_of_serine_protease_activity">Regulation of serine protease activity</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=10" title="Edit section: Regulation of serine protease activity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Host organisms must ensure that the activity of serine proteases is adequately regulated. This is achieved by a requirement for initial protease activation, and the secretion of inhibitors. </p> <div class="mw-heading mw-heading3"><h3 id="Zymogen_activation">Zymogen activation</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=11" title="Edit section: Zymogen activation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Zymogen" title="Zymogen">Zymogens</a> are the usually inactive precursors of an enzyme. If the digestive enzymes were active when synthesized, they would immediately start chewing up the synthesizing organs and tissues. <a href="/wiki/Acute_pancreatitis" title="Acute pancreatitis">Acute pancreatitis</a> is such a condition, in which there is premature activation of the digestive enzymes in the pancreas, resulting in self-digestion (autolysis). It also complicates <a href="/wiki/Postmortem_investigation" class="mw-redirect" title="Postmortem investigation">postmortem investigations</a>, as the pancreas often digests itself before it can be assessed visually. </p><p>Zymogens are large, inactive structures, which have the ability to break apart or change into the smaller activated enzymes. The difference between zymogens and the activated enzymes lies in the fact that the active site for catalysis of the zymogens is distorted. As a result, the substrate polypeptide cannot bind effectively, and <a href="/wiki/Proteolysis" title="Proteolysis">proteolysis</a> does not occur. Only after activation, during which the conformation and structure of the zymogen change and the active site is opened, can <a href="/wiki/Proteolysis" title="Proteolysis">proteolysis</a> occur. </p> <table class="wikitable"> <tbody><tr> <th>Zymogen </th> <th>Enzyme </th> <th>Notes </th></tr> <tr> <td><i>Trypsinogen</i></td> <td><a href="/wiki/Trypsin" title="Trypsin">trypsin</a></td> <td>When trypsinogen enters the <a href="/wiki/Small_intestine" title="Small intestine">small intestine</a> from the pancreas, <a href="/wiki/Enteropeptidase" title="Enteropeptidase">enteropeptidase</a> secretions from the duodenal mucosa cleave the lysine 15 - isoleucine 16 peptide bond of the zymogen. As a result, the zymogen trypsinogen breaks down into trypsin. Recall that trypsin is also responsible for cleaving <a href="/wiki/Lysine" title="Lysine">lysine</a> peptide bonds, and thus, once a small amount of trypsin is generated, it participates in cleavage of its own zymogen, generating even more trypsin. The process of trypsin activation can thus be called <a href="/wiki/Autocatalytic" class="mw-redirect" title="Autocatalytic">autocatalytic</a>. </td></tr> <tr> <td><i>Chymotrypsinogen</i></td> <td><a href="/wiki/Chymotrypsin" title="Chymotrypsin">chymotrypsin</a></td> <td>After the Arg 15 - Ile 16 bond in the chymotrypsinogen zymogen is cleaved by trypsin, the newly generated structure called a <i>pi-chymotrypsin</i> undergoes <a href="/wiki/Autolysis_(biology)" title="Autolysis (biology)">autolysis</a> (self digestion), yielding active chymotrypsin. </td></tr> <tr> <td><i>Proelastase</i></td> <td><a href="/wiki/Elastase" title="Elastase">elastase</a></td> <td>It is activated by cleavage through trypsin. </td></tr></tbody></table> <p>As can be seen, trypsinogen activation to <i>trypsin</i> is essential, because it activates its own reaction, as well as the reaction of both <i>chymotrypsin</i> and <i>elastase</i>. Therefore, it is essential that this activation does not occur prematurely. There are several protective measures taken by the organism to prevent self-digestion: </p> <ul><li>The activation of trypsinogen by trypsin is relatively slow</li> <li>The zymogens are stored in zymogen granules, capsules that have walls that are thought to be resistant to proteolysis.</li></ul> <div class="mw-heading mw-heading3"><h3 id="Inhibition">Inhibition</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=12" title="Edit section: Inhibition"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>There are certain <a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">inhibitors</a> that resemble the tetrahedral intermediate, and thus fill up the active site, preventing the enzyme from working properly. Trypsin, a powerful digestive enzyme, is generated in the pancreas. Inhibitors prevent self-digestion of the pancreas itself. </p><p>Serine proteases are paired with serine protease <a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">inhibitors</a>, which turn off their activity when they are no longer needed.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup><sup class="noprint Inline-Template" style="white-space:nowrap;">[<i><a href="/wiki/Wikipedia:Verifiability#Self-published_sources" title="Wikipedia:Verifiability"><span title="The material near this tag may rely on a self-published source. (May 2011)">self-published source?</span></a></i>]</sup> </p><p>Serine proteases are inhibited by a diverse group of <a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">inhibitors</a>, including synthetic chemical inhibitors for research or therapeutic purposes, and also natural proteinaceous inhibitors. One family of natural inhibitors called "serpins" (abbreviated from <a href="/wiki/Serine_protease_inhibitor" class="mw-redirect" title="Serine protease inhibitor">serine protease inhibitors</a>) can form a <a href="/wiki/Covalent" class="mw-redirect" title="Covalent">covalent</a> bond with the serine protease, inhibiting its function. The best-studied <i>serpins</i> are <a href="/wiki/Antithrombin" title="Antithrombin">antithrombin</a> and <a href="/wiki/Alpha_1-antitrypsin" class="mw-redirect" title="Alpha 1-antitrypsin">alpha 1-antitrypsin</a>, studied for their role in <a href="/wiki/Coagulation" title="Coagulation">coagulation</a>/<a href="/wiki/Thrombosis" title="Thrombosis">thrombosis</a> and <a href="/wiki/Emphysema" title="Emphysema">emphysema</a>/<a href="/wiki/A1AT" class="mw-redirect" title="A1AT">A1AT</a>, respectively. Artificial irreversible small molecule inhibitors include <a href="/wiki/AEBSF" title="AEBSF">AEBSF</a> and <a href="/wiki/PMSF" title="PMSF">PMSF</a>. </p><p>A family of <a href="/wiki/Arthropod" title="Arthropod">arthropod</a> serine peptidase inhibitors, called <a href="/wiki/Pacifastin" title="Pacifastin">pacifastin</a>, has been identified in <a href="/wiki/Locust" title="Locust">locusts</a> and <a href="/wiki/Crayfish" title="Crayfish">crayfish</a>, and may function in the arthropod <a href="/wiki/Immune_system" title="Immune system">immune system</a>.<sup id="cite_ref-pmid18775459_10-0" class="reference"><a href="#cite_note-pmid18775459-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Role_in_disease">Role in disease</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=13" title="Edit section: Role in disease"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Mutations may lead to decreased or increased activity of enzymes. This may have different consequences, depending on the normal function of the serine protease. For example, mutations in <a href="/wiki/Protein_C" title="Protein C">protein C</a> can lead to <a href="/wiki/Protein_C_deficiency" title="Protein C deficiency">protein C deficiency</a> and predisposing to <a href="/wiki/Thrombosis" title="Thrombosis">thrombosis</a>. Also, some proteases play a vital role in host cell-virus fusion activation by priming virus's Spike protein to show the protein named "fusion protein" (<a href="/wiki/TMPRSS2" title="TMPRSS2">TMPRSS2</a> activate <a href="/wiki/Severe_acute_respiratory_syndrome_coronavirus_2" class="mw-redirect" title="Severe acute respiratory syndrome coronavirus 2">SARS-CoV-2</a> fusion). Exogenous snake venom serine proteases cause a vast array of coagulopathies when injected in a host due to the lack of regulation of their activity.<sup id="cite_ref-:0_7-1" class="reference"><a href="#cite_note-:0-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Diagnostic_use">Diagnostic use</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=14" title="Edit section: Diagnostic use"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Determination of serine protease levels may be useful in the context of particular diseases. </p> <ul><li><a href="/wiki/Coagulation_factor" class="mw-redirect" title="Coagulation factor">Coagulation factor</a> levels may be required in the diagnosis of hemorrhagic or thrombotic conditions.</li> <li><a href="/wiki/Fecal_elastase" class="mw-redirect" title="Fecal elastase">Fecal elastase</a> is employed to determine the exocrine activity of the pancreas, e.g., in <a href="/wiki/Cystic_fibrosis" title="Cystic fibrosis">cystic fibrosis</a> or <a href="/wiki/Chronic_pancreatitis" title="Chronic pancreatitis">chronic pancreatitis</a>.</li> <li>Serum <a href="/wiki/Prostate-specific_antigen" title="Prostate-specific antigen">prostate-specific antigen</a> is used in <a href="/wiki/Prostate_cancer_screening" title="Prostate cancer screening">prostate cancer screening</a>, risk stratification, and post-treatment monitoring.</li> <li>Serine protease, as released by <a href="/wiki/Mast_cells" class="mw-redirect" title="Mast cells">mast cells</a>, is an important diagnostic marker for <a href="/wiki/Type_1_hypersensitivity" class="mw-redirect" title="Type 1 hypersensitivity">type 1 hypersensitivity</a> reactions e.g., <a href="/wiki/Anaphylaxis" title="Anaphylaxis">anaphylaxis</a>. More useful than <a href="/wiki/Histamine" title="Histamine">histamine</a> due to the longer <a href="/wiki/Half-life" title="Half-life">half-life</a>, meaning it remains in the system for a clinically useful length of time.</li></ul> <div class="mw-heading mw-heading2"><h2 id="Antimicrobial_effect">Antimicrobial effect</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=15" title="Edit section: Antimicrobial effect"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Due to their catalytic activity, some serine proteases possess potent antimicrobial properties. Several in vitro studies have demonstrated the efficacy of some proteases in reducing virulence by cleaving viral surface proteins. Viral entry into host cells is mediated by the interaction of these surface proteins with the host cell. When these proteins are fragmented or inactivated on the viral surface, the viral entry is impaired, leading to a reduction in infectivity of a broad spectrum of pathologically relevant microorganisms like <a href="/wiki/Influenza" title="Influenza">Influenza</a>, <a href="/wiki/HRSV" class="mw-redirect" title="HRSV">hRSV</a> and others.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=16" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1184024115">.mw-parser-output .div-col{margin-top:0.3em;column-width:30em}.mw-parser-output .div-col-small{font-size:90%}.mw-parser-output .div-col-rules{column-rule:1px solid #aaa}.mw-parser-output .div-col dl,.mw-parser-output .div-col ol,.mw-parser-output .div-col ul{margin-top:0}.mw-parser-output .div-col li,.mw-parser-output .div-col dd{page-break-inside:avoid;break-inside:avoid-column}</style><div class="div-col"> <ul><li><a href="/wiki/Serine_hydrolase" title="Serine hydrolase">Serine hydrolase</a></li> <li><a href="/wiki/Protease" title="Protease">Protease</a> <ul><li><a href="/wiki/Cysteine_protease" title="Cysteine protease">cysteine-</a></li> <li><a href="/wiki/Threonine_protease" title="Threonine protease">threonine-</a></li> <li><a href="/wiki/Aspartic_protease" title="Aspartic protease">aspartic-</a></li> <li><a href="/wiki/Metalloprotease" class="mw-redirect" title="Metalloprotease">metallo-</a></li></ul></li> <li><a href="/wiki/PA_clan" class="mw-redirect" title="PA clan">PA clan</a></li> <li><a href="/wiki/Convergent_evolution" title="Convergent evolution">Convergent evolution</a></li> <li><a href="/wiki/Proteolysis" title="Proteolysis">Proteolysis</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/The_Proteolysis_Map" title="The Proteolysis Map">The Proteolysis Map</a></li> <li><a href="/wiki/Proteases_in_angiogenesis" title="Proteases in angiogenesis">Proteases in angiogenesis</a></li> <li><a href="/wiki/Intramembrane_protease" title="Intramembrane protease">Intramembrane proteases</a></li> <li><a href="/wiki/Protease_inhibitor_(pharmacology)" title="Protease inhibitor (pharmacology)">Protease inhibitor (pharmacology)</a></li> <li><a href="/wiki/Protease_inhibitor_(biology)" title="Protease inhibitor (biology)">Protease inhibitor (biology)</a></li> <li><a href="/wiki/TopFIND" title="TopFIND">TopFIND</a> - database of protease specificity, substrates, products and inhibitors</li> <li><a href="/wiki/MEROPS" title="MEROPS">MEROPS</a> - Database of protease evolutionary groups</li> <li><a href="/wiki/Keratinase" title="Keratinase">Keratinase</a></li> <li><a href="/wiki/Subtilisin" title="Subtilisin">Subtilisin</a></li> <li><a href="/wiki/Proteinase_K" title="Proteinase K">Proteinase K</a></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=17" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></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-Hedstrom2002-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-Hedstrom2002_1-0">^</a></b></span> <span class="reference-text"> <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="CITEREFHedstrom2002" class="citation journal cs1">Hedstrom L (December 2002). 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class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Serine_protease&action=edit&section=18" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li>The <a href="/wiki/MEROPS" title="MEROPS">MEROPS</a> online database for peptidases and their inhibitors: <a rel="nofollow" class="external text" href="http://merops.sanger.ac.uk/cgi-bin/family_index?type=P#S">Serine Peptidase</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20170404112415/http://merops.sanger.ac.uk/cgi-bin/family_index?type=P#S">Archived</a> 2017-04-04 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a></li> <li><a rel="nofollow" class="external text" href="http://biochem.slu.edu/services/serprodb/">Serine Proteases</a> site at <a href="/wiki/Saint_Louis_University" title="Saint Louis University">Saint Louis University</a> (SLU)</li> <li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Serine+proteases">Serine+proteases</a> at the U.S. National Library of Medicine <a href="/wiki/Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</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 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.navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Hydrolase:_proteases_(EC_3.4)" 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:Proteases" title="Template:Proteases"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Proteases" title="Template talk:Proteases"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Proteases" title="Special:EditPage/Template:Proteases"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Hydrolase:_proteases_(EC_3.4)" style="font-size:114%;margin:0 4em"><a href="/wiki/Hydrolase" title="Hydrolase">Hydrolase</a>: <a href="/wiki/Protease" title="Protease">proteases</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> 3.4)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.11_Aminopeptidases" title="List of EC numbers (EC 3)">3.4.11</a>-19: <a href="/wiki/Exopeptidase" title="Exopeptidase">Exopeptidase</a></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/List_of_EC_numbers_(EC_3)#EC_3.4.11_Aminopeptidases" title="List of EC numbers (EC 3)">3.4.11</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 href="/wiki/Aminopeptidase" title="Aminopeptidase">Aminopeptidase</a> <ul><li><a href="/wiki/Alanine_aminopeptidase" title="Alanine aminopeptidase">Alanine</a></li> <li><a href="/wiki/RNPEP" title="RNPEP">Arginyl</a></li> <li><a href="/wiki/DNPEP" title="DNPEP">Aspartyl</a></li> <li><a href="/wiki/Cystinyl_aminopeptidase" class="mw-redirect" title="Cystinyl aminopeptidase">Cystinyl</a></li> <li><a href="/wiki/Leucyl_aminopeptidase" title="Leucyl aminopeptidase">Leucyl</a></li> <li><a href="/wiki/Glutamyl_aminopeptidase" title="Glutamyl aminopeptidase">Glutamyl</a></li> <li><i>Methionyl</i> <ul><li><a href="/wiki/METAP1" title="METAP1">1</a></li> <li><a href="/wiki/METAP2" title="METAP2">2</a></li></ul></li> <li><a href="/wiki/C9orf3" title="C9orf3">O</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.13_Dipeptidases" title="List of EC numbers (EC 3)">3.4.13</a></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/Dipeptidase" title="Dipeptidase">Dipeptidase</a> <ul><li><a href="/wiki/Dipeptidase_1" title="Dipeptidase 1">1</a></li> <li><a href="/wiki/DPEP2" class="mw-redirect" title="DPEP2">2</a></li> <li><a href="/wiki/DPEP3" class="mw-redirect" title="DPEP3">3</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.14_Dipeptidyl_peptidases_and_tripeptidyl_peptidases" title="List of EC numbers (EC 3)">3.4.14</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 href="/wiki/Dipeptidyl_peptidase" title="Dipeptidyl peptidase">Dipeptidyl peptidase</a> <ul><li><a href="/wiki/Cathepsin_C" title="Cathepsin C">Cathepsin C</a></li> <li><a href="/wiki/Dipeptidyl_peptidase-4" title="Dipeptidyl peptidase-4">Dipeptidyl peptidase-4</a></li></ul></li> <li><a href="/wiki/Tripeptidyl_peptidase" title="Tripeptidyl peptidase">Tripeptidyl peptidase</a> <ul><li><a href="/wiki/Tripeptidyl_peptidase_I" title="Tripeptidyl peptidase I">Tripeptidyl peptidase I</a></li> <li><a href="/wiki/Tripeptidyl_peptidase_II" title="Tripeptidyl peptidase II">Tripeptidyl peptidase II</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.15_Peptidyl_dipeptidases" title="List of EC numbers (EC 3)">3.4.15</a></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/Angiotensin-converting_enzyme" title="Angiotensin-converting enzyme">Angiotensin-converting enzyme</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.16_Serine_type_carboxypeptidases" title="List of EC numbers (EC 3)">3.4.16</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 href="/wiki/Serine_type_carboxypeptidase" class="mw-redirect" title="Serine type carboxypeptidase">Serine type carboxypeptidases</a>: <a href="/wiki/Cathepsin_A" title="Cathepsin A">Cathepsin A</a></li> <li><a href="/wiki/DD-Transpeptidase" title="DD-Transpeptidase"><small>DD</small>-Transpeptidase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.17_Metallocarboxypeptidases" title="List of EC numbers (EC 3)">3.4.17</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <dl><dt><span class="nobold"><a href="/wiki/Metalloexopeptidase" title="Metalloexopeptidase">Metalloexopeptidases</a></span></dt> <dd><a href="/wiki/Carboxypeptidase" title="Carboxypeptidase">Carboxypeptidase</a> <dl><dd><a href="/wiki/Carboxypeptidase_A" title="Carboxypeptidase A">A</a></dd> <dd><a href="/wiki/Carboxypeptidase_A2" title="Carboxypeptidase A2">A2</a></dd> <dd><a href="/wiki/Carboxypeptidase_B" title="Carboxypeptidase B">B</a></dd> <dd><a href="/wiki/Cathepsin_A" title="Cathepsin A">C</a></dd> <dd><a href="/wiki/Carboxypeptidase_E" title="Carboxypeptidase E">E</a></dd> <dd><a href="/wiki/Glutamate_carboxypeptidase_II" title="Glutamate carboxypeptidase II">Glutamate II</a></dd></dl></dd></dl> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other/ungrouped</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 href="/wiki/Metalloexopeptidase" title="Metalloexopeptidase">Metalloexopeptidase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.21:_Serine_proteases" title="List of EC numbers (EC 3)">3.4.21</a>-25: <a href="/wiki/Endopeptidase" title="Endopeptidase">Endopeptidase</a></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 class="mw-selflink selflink">Serine protease</a></li> <li><a href="/wiki/Cysteine_protease" title="Cysteine protease">Cysteine protease</a></li> <li><a href="/wiki/Aspartate_protease" class="mw-redirect" title="Aspartate protease">Aspartic acid protease</a></li> <li><a href="/wiki/Metalloendopeptidase" title="Metalloendopeptidase">Metalloendopeptidase</a></li> <li><a href="/wiki/Threonine_endopeptidase" class="mw-redirect" title="Threonine endopeptidase">Threonine endopeptidase</a> <ul><li><a href="/wiki/Proteasome_endopeptidase_complex" title="Proteasome endopeptidase complex">Proteasome endopeptidase complex</a></li> <li><a href="/wiki/HslU%E2%80%94HslV_peptidase" class="mw-redirect" title="HslU—HslV peptidase">HslU—HslV peptidase</a></li></ul></li></ul> <ul><li>Other/ungrouped: <a href="/wiki/Amyloid_precursor_protein_secretase" class="mw-redirect" title="Amyloid precursor protein secretase">Amyloid precursor protein secretase</a> <ul><li><a href="/wiki/Alpha_secretase" title="Alpha secretase">Alpha secretase</a></li> <li><a href="/wiki/Beta-secretase_1" title="Beta-secretase 1">Beta-secretase 1</a></li> <li><a href="/wiki/Beta-secretase_2" title="Beta-secretase 2">Beta-secretase 2</a></li> <li><a href="/wiki/Gamma_secretase" title="Gamma secretase">Gamma secretase</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.99_Endopeptidases_of_unknown_catalytic_mechanism" title="List of EC numbers (EC 3)">3.4.99</a>: Unknown</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/Staphylokinase" title="Staphylokinase">Staphylokinase</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="Endopeptidases:_serine_proteases/serine_endopeptidases_(EC_3.4.21)" 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:Serine_endopeptidases" title="Template:Serine endopeptidases"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Serine_endopeptidases" title="Template talk:Serine endopeptidases"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Serine_endopeptidases" title="Special:EditPage/Template:Serine endopeptidases"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Endopeptidases:_serine_proteases/serine_endopeptidases_(EC_3.4.21)" style="font-size:114%;margin:0 4em"><a href="/wiki/Endopeptidase" title="Endopeptidase">Endopeptidases</a>: <a class="mw-selflink selflink">serine proteases/serine endopeptidases</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> <a href="/wiki/List_of_EC_numbers_(EC_3)#EC_3.4.21:_Serine_proteases" title="List of EC numbers (EC 3)">3.4.21</a>)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Digestive_enzyme" title="Digestive enzyme">Digestive enzymes</a></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/Enteropeptidase" title="Enteropeptidase">Enteropeptidase</a></li> <li><a href="/wiki/Trypsin" title="Trypsin">Trypsin</a></li> <li><a href="/wiki/Chymotrypsin" title="Chymotrypsin">Chymotrypsin</a></li> <li><a href="/wiki/Elastase" title="Elastase">Elastase</a> <ul><li><a href="/wiki/Neutrophil_elastase" title="Neutrophil elastase">Neutrophil</a></li> <li><a href="/wiki/Pancreatic_elastase" title="Pancreatic elastase">Pancreatic</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Coagulation" title="Coagulation">Coagulation</a></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><i>factors:</i> <a href="/wiki/Thrombin" title="Thrombin">Thrombin</a></li> <li><a href="/wiki/Factor_VII" title="Factor VII">Factor VIIa</a></li> <li><a href="/wiki/Factor_IX" title="Factor IX">Factor IXa</a></li> <li><a href="/wiki/Factor_X" title="Factor X">Factor Xa</a></li> <li><a href="/wiki/Factor_XI" title="Factor XI">Factor XIa</a></li> <li><a href="/wiki/Factor_XII" title="Factor XII">Factor XIIa</a></li> <li><a href="/wiki/Kallikrein" title="Kallikrein">Kallikrein</a> <ul><li><a href="/wiki/Prostate-specific_antigen" title="Prostate-specific antigen">PSA</a></li> <li><a href="/wiki/KLK1" title="KLK1">KLK1</a></li> <li><a href="/wiki/KLK2" title="KLK2">KLK2</a></li> <li><a href="/wiki/Prostate-specific_antigen" title="Prostate-specific antigen">KLK3</a></li> <li><a href="/wiki/KLK4" title="KLK4">KLK4</a></li> <li><a href="/wiki/KLK5" class="mw-redirect" title="KLK5">KLK5</a></li> <li><a href="/wiki/KLK6" title="KLK6">KLK6</a></li> <li><a href="/wiki/KLK7" title="KLK7">KLK7</a></li> <li><a href="/wiki/KLK8" title="KLK8">KLK8</a></li> <li><a href="/wiki/KLK9" title="KLK9">KLK9</a></li> <li><a href="/wiki/KLK10" title="KLK10">KLK10</a></li> <li><a href="/wiki/KLK11" title="KLK11">KLK11</a></li> <li><a href="/wiki/KLK12" title="KLK12">KLK12</a></li> <li><a href="/wiki/KLK13" title="KLK13">KLK13</a></li> <li><a href="/wiki/KLK14" title="KLK14">KLK14</a></li> <li><a href="/wiki/KLK15" title="KLK15">KLK15</a></li></ul></li></ul> <ul><li><i><a href="/wiki/Fibrinolysis" title="Fibrinolysis">fibrinolysis</a>:</i> <a href="/wiki/Plasmin" title="Plasmin">Plasmin</a></li> <li><a href="/wiki/Plasminogen_activator" title="Plasminogen activator">Plasminogen activator</a> <ul><li><a href="/wiki/Tissue_plasminogen_activator" class="mw-redirect" title="Tissue plasminogen activator">Tissue plasminogen activator</a></li> <li><a href="/wiki/Urokinase" title="Urokinase">Urinary plasminogen activator</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Complement_system" title="Complement system">Complement system</a></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/Complement_factor_B" title="Complement factor B">Factor B</a></li> <li><a href="/wiki/Factor_D" title="Factor D">Factor D</a></li> <li><a href="/wiki/Complement_factor_I" title="Complement factor I">Factor I</a></li> <li><a href="/wiki/Mannose-binding_protein-associated_serine_protease" title="Mannose-binding protein-associated serine protease">MASP</a> <ul><li><a href="/wiki/MASP1_(protein)" title="MASP1 (protein)">MASP1</a></li> <li><a href="/wiki/MASP2_(protein)" title="MASP2 (protein)">MASP2</a></li></ul></li> <li><a href="/wiki/C3-convertase" title="C3-convertase">C3-convertase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other <a href="/wiki/Immune_system" title="Immune system">immune system</a></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/Chymase" title="Chymase">Chymase</a></li> <li><a href="/wiki/Granzyme" title="Granzyme">Granzyme</a></li> <li><a href="/wiki/Tryptase" title="Tryptase">Tryptase</a></li> <li><a href="/wiki/Proteinase_3" title="Proteinase 3">Proteinase 3/Myeloblastin</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Venom" title="Venom">Venombin</a></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/Ancrod" title="Ancrod">Ancrod</a></li> <li><a href="/wiki/Batroxobin" title="Batroxobin">Batroxobin</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</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/Acrosin" title="Acrosin">Acrosin</a></li> <li><a href="/wiki/Prolyl_endopeptidase" title="Prolyl endopeptidase">Prolyl endopeptidase</a></li> <li><a href="/wiki/Pronase" title="Pronase">Pronase</a></li> <li><a href="/wiki/Proprotein_convertase" title="Proprotein convertase">Proprotein convertases</a> <ul><li><a href="/wiki/Proprotein_convertase_1" title="Proprotein convertase 1">1</a></li> <li><a href="/wiki/Proprotein_convertase_2" title="Proprotein convertase 2">2</a></li></ul></li> <li><a href="/wiki/PRSS8" title="PRSS8">Prostasin</a></li> <li><a href="/wiki/Reelin" title="Reelin">Reelin</a></li> <li><a href="/wiki/Subtilisin" title="Subtilisin">Subtilisin</a>/<a href="/wiki/Furin" title="Furin">Furin</a>/<a href="/wiki/Membrane-bound_transcription_factor_peptidase,_site_1" class="mw-redirect" title="Membrane-bound transcription factor peptidase, site 1">S1P</a>4</li> <li><a href="/wiki/Sedolisin" title="Sedolisin">Sedolisin</a>/<a href="/wiki/Tripeptidyl_peptidase_I" title="Tripeptidyl peptidase I">TPP1</a></li> <li><a href="/wiki/Streptokinase" title="Streptokinase">Streptokinase</a></li> <li><a href="/wiki/Cathepsin" title="Cathepsin">Cathepsin</a> <ul><li><a href="/wiki/Cathepsin_A" title="Cathepsin A">A</a></li> <li><a href="/wiki/Cathepsin_G" title="Cathepsin G">G</a></li></ul></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="Enzymes" 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="Enzymes" 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 href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">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><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li><b>EC7 <a 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