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Cofactor (biochemistry) - Wikipedia

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<span class="vector-toc-numb">2</span> <span>Inorganic cofactors</span> </div> </a> <button aria-controls="toc-Inorganic_cofactors-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 Inorganic cofactors subsection</span> </button> <ul id="toc-Inorganic_cofactors-sublist" class="vector-toc-list"> <li id="toc-Metal_ions" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Metal_ions"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>Metal ions</span> </div> </a> <ul id="toc-Metal_ions-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Iron–sulfur_clusters" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Iron–sulfur_clusters"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>Iron–sulfur clusters</span> </div> </a> <ul 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id="toc-Non-vitamins" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Non-vitamins"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>Non-vitamins</span> </div> </a> <ul id="toc-Non-vitamins-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cofactors_as_metabolic_intermediates" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cofactors_as_metabolic_intermediates"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>Cofactors as metabolic intermediates</span> </div> </a> <ul id="toc-Cofactors_as_metabolic_intermediates-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Evolution" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Evolution"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.4</span> <span>Evolution</span> </div> </a> <ul id="toc-Evolution-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-History" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#History"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.5</span> <span>History</span> </div> </a> <ul id="toc-History-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Protein-derived_cofactors" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Protein-derived_cofactors"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Protein-derived cofactors</span> </div> </a> <ul id="toc-Protein-derived_cofactors-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Non-enzymatic_cofactors" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Non-enzymatic_cofactors"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Non-enzymatic cofactors</span> </div> </a> <ul id="toc-Non-enzymatic_cofactors-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">6</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">7</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Further_reading" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Further_reading"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Further reading</span> </div> </a> <ul id="toc-Further_reading-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">9</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">Cofactor (biochemistry)</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 45 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-45" 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">45 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%B9%D8%A7%D9%85%D9%84_%D9%85%D8%B1%D8%A7%D9%81%D9%82_(%D9%83%D9%8A%D9%85%D9%8A%D8%A7%D8%A1_%D8%AD%D9%8A%D9%88%D9%8A%D8%A9)" title="عامل مرافق (كيمياء حيوية) – Arabic" lang="ar" hreflang="ar" data-title="عامل مرافق (كيمياء حيوية)" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bg mw-list-item"><a href="https://bg.wikipedia.org/wiki/%D0%9A%D0%BE%D1%84%D0%B0%D0%BA%D1%82%D0%BE%D1%80" title="Кофактор – Bulgarian" lang="bg" hreflang="bg" data-title="Кофактор" data-language-autonym="Български" data-language-local-name="Bulgarian" class="interlanguage-link-target"><span>Български</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Cofactor_enzim%C3%A0tic" title="Cofactor enzimàtic – Catalan" lang="ca" hreflang="ca" data-title="Cofactor enzimàtic" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Kofaktor_(biochemie)" title="Kofaktor (biochemie) – Czech" lang="cs" hreflang="cs" data-title="Kofaktor (biochemie)" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Cofaktor" title="Cofaktor – Danish" lang="da" hreflang="da" data-title="Cofaktor" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target"><span>Dansk</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Cofaktor_(Biochemie)" title="Cofaktor (Biochemie) – German" lang="de" hreflang="de" data-title="Cofaktor (Biochemie)" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Kofaktor" title="Kofaktor – Estonian" lang="et" hreflang="et" data-title="Kofaktor" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target"><span>Eesti</span></a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%A3%CF%85%CE%BC%CF%80%CE%B1%CF%81%CE%AC%CE%B3%CE%BF%CE%BD%CF%84%CE%B1%CF%82_(%CE%B2%CE%B9%CE%BF%CF%87%CE%B7%CE%BC%CE%B5%CE%AF%CE%B1)" title="Συμπαράγοντας (βιοχημεία) – Greek" lang="el" hreflang="el" data-title="Συμπαράγοντας (βιοχημεία)" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target"><span>Ελληνικά</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Cofactor" title="Cofactor – Spanish" lang="es" hreflang="es" data-title="Cofactor" 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/%DA%A9%D9%88%D9%81%D8%A7%DA%A9%D8%AA%D9%88%D8%B1_(%D8%A8%DB%8C%D9%88%D8%B4%DB%8C%D9%85%DB%8C)" title="کوفاکتور (بیوشیمی) – Persian" lang="fa" hreflang="fa" data-title="کوفاکتور (بیوشیمی)" 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/Cofacteur_(biochimie)" title="Cofacteur (biochimie) – French" lang="fr" hreflang="fr" data-title="Cofacteur (biochimie)" 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/Cofactor" title="Cofactor – Galician" lang="gl" hreflang="gl" data-title="Cofactor" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EB%B3%B4%EC%A1%B0_%EC%9D%B8%EC%9E%90" title="보조 인자 – Korean" lang="ko" hreflang="ko" data-title="보조 인자" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-hi mw-list-item"><a href="https://hi.wikipedia.org/wiki/%E0%A4%B8%E0%A4%B9%E0%A4%95%E0%A4%BE%E0%A4%B0%E0%A4%95_(%E0%A4%9C%E0%A5%88%E0%A4%B5%E0%A4%B0%E0%A4%B8%E0%A4%BE%E0%A4%AF%E0%A4%A8)" title="सहकारक (जैवरसायन) – Hindi" lang="hi" hreflang="hi" data-title="सहकारक (जैवरसायन)" data-language-autonym="हिन्दी" data-language-local-name="Hindi" class="interlanguage-link-target"><span>हिन्दी</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Kofaktor_(biokimia)" title="Kofaktor (biokimia) – Indonesian" lang="id" hreflang="id" data-title="Kofaktor (biokimia)" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Cofattore_(biologia)" title="Cofattore (biologia) – Italian" lang="it" hreflang="it" data-title="Cofattore (biologia)" 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%A7%D7%95%D7%A4%D7%A7%D7%98%D7%95%D7%A8" title="קופקטור – Hebrew" lang="he" hreflang="he" data-title="קופקטור" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-ka mw-list-item"><a href="https://ka.wikipedia.org/wiki/%E1%83%99%E1%83%9D%E1%83%A4%E1%83%90%E1%83%A5%E1%83%A2%E1%83%9D%E1%83%A0%E1%83%94%E1%83%91%E1%83%98" title="კოფაქტორები – Georgian" lang="ka" hreflang="ka" data-title="კოფაქტორები" data-language-autonym="ქართული" data-language-local-name="Georgian" class="interlanguage-link-target"><span>ქართული</span></a></li><li class="interlanguage-link interwiki-kk mw-list-item"><a href="https://kk.wikipedia.org/wiki/%D0%9A%D0%BE%D1%84%D0%B0%D0%BA%D1%82%D0%BE%D1%80" title="Кофактор – Kazakh" lang="kk" hreflang="kk" data-title="Кофактор" data-language-autonym="Қазақша" data-language-local-name="Kazakh" class="interlanguage-link-target"><span>Қазақша</span></a></li><li class="interlanguage-link interwiki-la mw-list-item"><a href="https://la.wikipedia.org/wiki/Cofactor_(biochemia)" title="Cofactor (biochemia) – Latin" lang="la" hreflang="la" data-title="Cofactor (biochemia)" data-language-autonym="Latina" data-language-local-name="Latin" class="interlanguage-link-target"><span>Latina</span></a></li><li class="interlanguage-link interwiki-lt mw-list-item"><a href="https://lt.wikipedia.org/wiki/Kofaktorius" title="Kofaktorius – Lithuanian" lang="lt" hreflang="lt" data-title="Kofaktorius" data-language-autonym="Lietuvių" data-language-local-name="Lithuanian" class="interlanguage-link-target"><span>Lietuvių</span></a></li><li class="interlanguage-link interwiki-hu mw-list-item"><a href="https://hu.wikipedia.org/wiki/Kofaktor" title="Kofaktor – Hungarian" lang="hu" hreflang="hu" data-title="Kofaktor" data-language-autonym="Magyar" data-language-local-name="Hungarian" class="interlanguage-link-target"><span>Magyar</span></a></li><li class="interlanguage-link interwiki-mk mw-list-item"><a href="https://mk.wikipedia.org/wiki/%D0%9A%D0%BE%D1%84%D0%B0%D0%BA%D1%82%D0%BE%D1%80_(%D0%B1%D0%B8%D0%BE%D1%85%D0%B5%D0%BC%D0%B8%D1%98%D0%B0)" title="Кофактор (биохемија) – Macedonian" lang="mk" hreflang="mk" data-title="Кофактор (биохемија)" data-language-autonym="Македонски" data-language-local-name="Macedonian" class="interlanguage-link-target"><span>Македонски</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Kofaktor_(biokimia)" title="Kofaktor (biokimia) – Malay" lang="ms" hreflang="ms" data-title="Kofaktor (biokimia)" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target"><span>Bahasa Melayu</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Cofactor_(biochemie)" title="Cofactor (biochemie) – Dutch" lang="nl" hreflang="nl" data-title="Cofactor (biochemie)" 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/%E8%A3%9C%E5%9B%A0%E5%AD%90" title="補因子 – Japanese" lang="ja" hreflang="ja" data-title="補因子" 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-no mw-list-item"><a href="https://no.wikipedia.org/wiki/Kofaktor" title="Kofaktor – Norwegian Bokmål" lang="nb" hreflang="nb" data-title="Kofaktor" data-language-autonym="Norsk bokmål" data-language-local-name="Norwegian Bokmål" class="interlanguage-link-target"><span>Norsk bokmål</span></a></li><li class="interlanguage-link interwiki-oc mw-list-item"><a href="https://oc.wikipedia.org/wiki/Cofactor_(bioquimia)" title="Cofactor (bioquimia) – Occitan" lang="oc" hreflang="oc" data-title="Cofactor (bioquimia)" data-language-autonym="Occitan" data-language-local-name="Occitan" class="interlanguage-link-target"><span>Occitan</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Kofaktory" title="Kofaktory – Polish" lang="pl" hreflang="pl" data-title="Kofaktory" 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/Cofator_(bioqu%C3%ADmica)" title="Cofator (bioquímica) – Portuguese" lang="pt" hreflang="pt" data-title="Cofator (bioquímica)" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Cofactor" title="Cofactor – Romanian" lang="ro" hreflang="ro" data-title="Cofactor" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target"><span>Română</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%9A%D0%BE%D1%84%D0%B0%D0%BA%D1%82%D0%BE%D1%80" title="Кофактор – Russian" lang="ru" hreflang="ru" data-title="Кофактор" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sq mw-list-item"><a href="https://sq.wikipedia.org/wiki/Kofaktor_(biokimi)" title="Kofaktor (biokimi) – Albanian" lang="sq" hreflang="sq" data-title="Kofaktor (biokimi)" data-language-autonym="Shqip" data-language-local-name="Albanian" class="interlanguage-link-target"><span>Shqip</span></a></li><li class="interlanguage-link interwiki-simple mw-list-item"><a href="https://simple.wikipedia.org/wiki/Co-factor" title="Co-factor – Simple English" lang="en-simple" hreflang="en-simple" data-title="Co-factor" data-language-autonym="Simple English" data-language-local-name="Simple English" class="interlanguage-link-target"><span>Simple English</span></a></li><li class="interlanguage-link interwiki-sk mw-list-item"><a href="https://sk.wikipedia.org/wiki/Kofaktor_(bioch%C3%A9mia)" title="Kofaktor (biochémia) – Slovak" lang="sk" hreflang="sk" data-title="Kofaktor (biochémia)" data-language-autonym="Slovenčina" data-language-local-name="Slovak" class="interlanguage-link-target"><span>Slovenčina</span></a></li><li class="interlanguage-link interwiki-sl mw-list-item"><a href="https://sl.wikipedia.org/wiki/Kofaktor" title="Kofaktor – Slovenian" lang="sl" hreflang="sl" data-title="Kofaktor" data-language-autonym="Slovenščina" data-language-local-name="Slovenian" class="interlanguage-link-target"><span>Slovenščina</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Kofaktor_(biohemija)" title="Kofaktor (biohemija) – Serbian" lang="sr" hreflang="sr" data-title="Kofaktor (biohemija)" 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-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Kofaktor_(biohemija)" title="Kofaktor (biohemija) – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Kofaktor (biohemija)" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Kofaktori" title="Kofaktori – Finnish" lang="fi" hreflang="fi" data-title="Kofaktori" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Kofaktor" title="Kofaktor – Swedish" lang="sv" hreflang="sv" data-title="Kofaktor" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B9%82%E0%B8%84%E0%B9%81%E0%B8%9F%E0%B8%81%E0%B9%80%E0%B8%95%E0%B8%AD%E0%B8%A3%E0%B9%8C" title="โคแฟกเตอร์ – Thai" lang="th" hreflang="th" data-title="โคแฟกเตอร์" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Kofakt%C3%B6r_(biyokimya)" title="Kofaktör (biyokimya) – Turkish" lang="tr" hreflang="tr" data-title="Kofaktör (biyokimya)" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%9A%D0%BE%D1%84%D0%B0%D0%BA%D1%82%D0%BE%D1%80" title="Кофактор – Ukrainian" lang="uk" hreflang="uk" 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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">Non-protein chemical compound or metallic ion</div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/9/97/Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png/300px-Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png" decoding="async" width="300" height="300" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/97/Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png/450px-Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/97/Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png/600px-Succinate_Dehydrogenase_1YQ3_Electron_Carriers_Labeled.png 2x" data-file-width="1620" data-file-height="1620" /></a><figcaption>The <a href="/wiki/Succinate_dehydrogenase" title="Succinate dehydrogenase">succinate dehydrogenase</a> complex showing several cofactors, including <a href="/wiki/Flavin_group" title="Flavin group">flavin</a>, <a href="/wiki/Iron%E2%80%93sulfur_protein" title="Iron–sulfur protein">iron–sulfur centers</a>, and <a href="/wiki/Heme" title="Heme">heme</a>.</figcaption></figure> <p>A <b>cofactor</b> is a non-<a href="/wiki/Protein" title="Protein">protein</a> <a href="/wiki/Chemical_compound" title="Chemical compound">chemical compound</a> or <a href="/wiki/Metal_ions_in_aqueous_solution" title="Metal ions in aqueous solution">metallic ion</a> that is required for an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a>'s role as a <a href="/wiki/Catalysis" title="Catalysis">catalyst</a> (a catalyst is a substance that increases the rate of a <a href="/wiki/Chemical_reaction" title="Chemical reaction">chemical reaction</a>). Cofactors can be considered "helper molecules" that assist in <a href="/wiki/Biochemistry" title="Biochemistry">biochemical</a> transformations. The rates at which these happen are characterized in an area of study called <a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">enzyme kinetics</a>. Cofactors typically differ from <a href="/wiki/Ligand_(biochemistry)" title="Ligand (biochemistry)">ligands</a> in that they often derive their function by remaining bound. </p><p>Cofactors can be classified into two types: <a href="/wiki/Inorganic_ions" title="Inorganic ions">inorganic ions</a> and complex <a href="/wiki/Organic_molecule" class="mw-redirect" title="Organic molecule">organic molecules</a> called <a href="/wiki/Enzyme#Coenzymes" title="Enzyme">coenzymes</a>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">&#91;</span>1<span class="cite-bracket">&#93;</span></a></sup> Coenzymes are mostly derived from <a href="/wiki/Vitamin" title="Vitamin">vitamins</a> and other organic <a href="/wiki/Essential_nutrient" class="mw-redirect" title="Essential nutrient">essential nutrients</a> in small amounts. (Some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">&#91;</span>2<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">&#91;</span>3<span class="cite-bracket">&#93;</span></a></sup>) </p><p>Coenzymes are further divided into two types. The first is called a "<a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic group</a>", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a protein.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">&#91;</span>4<span class="cite-bracket">&#93;</span></a></sup> The second type of coenzymes are called "cosubstrates", and are transiently bound to the protein. Cosubstrates may be released from a protein at some point, and then rebind later. Both prosthetic groups and cosubstrates have the same function, which is to facilitate the reaction of enzymes and proteins. An inactive enzyme without the cofactor is called an <a href="/wiki/Apoenzyme" class="mw-redirect" title="Apoenzyme">apoenzyme</a>, while the complete enzyme with cofactor is called a <a href="/wiki/Holoenzyme" class="mw-redirect" title="Holoenzyme">holoenzyme</a>.<sup id="cite_ref-Metzler_5-0" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup><sup class="noprint Inline-Template" style="white-space:nowrap;">&#91;<i><a href="/wiki/Wikipedia:Citing_sources" title="Wikipedia:Citing sources"><span title="This citation requires a reference to the specific page or range of pages in which the material appears. (October 2023)">page&#160;needed</span></a></i>&#93;</sup> </p><p>The <a href="/wiki/International_Union_of_Pure_and_Applied_Chemistry" title="International Union of Pure and Applied Chemistry">International Union of Pure and Applied Chemistry</a> (IUPAC) defines "coenzyme" a little differently, namely as a low-molecular-weight, non-protein organic compound that is loosely attached, participating in enzymatic reactions as a dissociable carrier of chemical groups or electrons; a prosthetic group is defined as a tightly bound, <a href="/wiki/Nonpolypeptide" class="mw-redirect" title="Nonpolypeptide">nonpolypeptide</a> unit in a protein that is regenerated in each enzymatic turnover.<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">&#91;</span>6<span class="cite-bracket">&#93;</span></a></sup> </p><p>Some enzymes or enzyme complexes require several cofactors. For example, the multienzyme complex <a href="/wiki/Pyruvate_dehydrogenase" title="Pyruvate dehydrogenase">pyruvate dehydrogenase</a><sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">&#91;</span>7<span class="cite-bracket">&#93;</span></a></sup> at the junction of <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a> and the <a href="/wiki/Citric_acid_cycle" title="Citric acid cycle">citric acid cycle</a> requires five organic cofactors and one metal ion: loosely bound <a href="/wiki/Thiamine_pyrophosphate" title="Thiamine pyrophosphate">thiamine pyrophosphate</a> (TPP), covalently bound <a href="/wiki/Lipoamide" title="Lipoamide">lipoamide</a> and <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">flavin adenine dinucleotide</a> (FAD), cosubstrates <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">nicotinamide adenine dinucleotide</a> (NAD<sup>+</sup>) and <a href="/wiki/Coenzyme_A" title="Coenzyme A">coenzyme A</a> (CoA), and a metal ion (Mg<sup>2+</sup>).<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">&#91;</span>8<span class="cite-bracket">&#93;</span></a></sup> </p><p>Organic cofactors are often <a href="/wiki/Vitamin" title="Vitamin">vitamins</a> or made from vitamins. Many contain the <a href="/wiki/Nucleotide" title="Nucleotide">nucleotide</a> <a href="/wiki/Adenosine_monophosphate" title="Adenosine monophosphate">adenosine monophosphate</a> (AMP) as part of their structures, such as <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>, <a href="/wiki/Coenzyme_A" title="Coenzyme A">coenzyme A</a>, <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">FAD</a>, and <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NAD<sup>+</sup></a>. This common structure may reflect a common evolutionary origin as part of <a href="/wiki/Ribozyme" title="Ribozyme">ribozymes</a> in an ancient <a href="/wiki/RNA_world_hypothesis" class="mw-redirect" title="RNA world hypothesis">RNA world</a>. It has been suggested that the AMP part of the molecule can be considered to be a kind of "handle" by which the enzyme can "grasp" the coenzyme to switch it between different catalytic centers.<sup id="cite_ref-Denessiouk_9-0" class="reference"><a href="#cite_note-Denessiouk-9"><span class="cite-bracket">&#91;</span>9<span class="cite-bracket">&#93;</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=Cofactor_(biochemistry)&amp;action=edit&amp;section=1" title="Edit section: Classification"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Cofactors can be divided into two major groups: <b>organic</b> <b>cofactors</b>, such as <a href="/wiki/Flavin_group" title="Flavin group">flavin</a> or <a href="/wiki/Heme" title="Heme">heme</a>; and <b>inorganic cofactors</b>, such as the metal ions Mg<sup>2+</sup>, Cu<sup>+</sup>, Mn<sup>2+</sup> and <a href="/wiki/Iron%E2%80%93sulfur_cluster" title="Iron–sulfur cluster">iron–sulfur clusters</a>. </p><p>Organic cofactors are sometimes further divided into <i>coenzymes</i> and <i><a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic groups</a></i>. The term coenzyme refers specifically to enzymes and, as such, to the functional properties of a protein. On the other hand, "prosthetic group" emphasizes the nature of the binding of a cofactor to a protein (tight or covalent) and, thus, refers to a structural property. Different sources give slightly different definitions of coenzymes, cofactors, and prosthetic groups. Some consider tightly bound organic molecules as prosthetic groups and not as coenzymes, while others define all non-protein organic molecules needed for enzyme activity as coenzymes, and classify those that are tightly bound as coenzyme prosthetic groups. These terms are often used loosely. </p><p>A 1980 letter in <i>Trends in Biochemistry Sciences</i> noted the confusion in the literature and the essentially arbitrary distinction made between prosthetic groups and coenzymes group and proposed the following scheme. Here, cofactors were defined as an additional substance apart from protein and <a href="/wiki/Enzyme_substrate" class="mw-redirect" title="Enzyme substrate">substrate</a> that is required for enzyme activity and a prosthetic group as a substance that undergoes its whole <a href="/wiki/Catalytic_cycle" title="Catalytic cycle">catalytic cycle</a> attached to a single enzyme molecule. However, the author could not arrive at a single all-encompassing definition of a "coenzyme" and proposed that this term be dropped from use in the literature.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">&#91;</span>10<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Inorganic_cofactors">Inorganic cofactors</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=2" title="Edit section: Inorganic cofactors"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Metal_ions">Metal ions</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=3" title="Edit section: Metal ions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Metalloprotein" title="Metalloprotein">Metalloprotein</a></div> <p><a href="/wiki/Metal" title="Metal">Metal</a> <a href="/wiki/Ion" title="Ion">ions</a> are common cofactors.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">&#91;</span>11<span class="cite-bracket">&#93;</span></a></sup> The study of these cofactors falls under the area of <a href="/wiki/Bioinorganic_chemistry" title="Bioinorganic chemistry">bioinorganic chemistry</a>. In <a href="/wiki/Nutrition" title="Nutrition">nutrition</a>, the list of essential <a href="/wiki/Trace_element" title="Trace element">trace elements</a> reflects their role as cofactors. In humans this list commonly includes <a href="/wiki/Iron" title="Iron">iron</a>, <a href="/wiki/Magnesium" title="Magnesium">magnesium</a>, <a href="/wiki/Manganese" title="Manganese">manganese</a>, <a href="/wiki/Cobalt" title="Cobalt">cobalt</a>, <a href="/wiki/Copper" title="Copper">copper</a>, <a href="/wiki/Zinc" title="Zinc">zinc</a>, and <a href="/wiki/Molybdenum" title="Molybdenum">molybdenum</a>.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">&#91;</span>12<span class="cite-bracket">&#93;</span></a></sup> Although <a href="/wiki/Chromium" title="Chromium">chromium</a> deficiency causes <a href="/wiki/Impaired_glucose_tolerance" class="mw-redirect" title="Impaired glucose tolerance">impaired glucose tolerance</a>, no human enzyme that uses this metal as a cofactor has been identified.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">&#91;</span>13<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">&#91;</span>14<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Iodine" title="Iodine">Iodine</a> is also an essential trace element, but this element is used as part of the structure of <a href="/wiki/Thyroid_hormone" class="mw-redirect" title="Thyroid hormone">thyroid hormones</a> rather than as an enzyme cofactor.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">&#91;</span>15<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Calcium" title="Calcium">Calcium</a> is another special case, in that it is required as a component of the human diet, and it is needed for the full activity of many enzymes, such as <a href="/wiki/Nitric_oxide_synthase" title="Nitric oxide synthase">nitric oxide synthase</a>, <a href="/wiki/Phosphatase" title="Phosphatase">protein phosphatases</a>, and <a href="/wiki/Adenylate_kinase" title="Adenylate kinase">adenylate kinase</a>, but calcium activates these enzymes in <a href="/wiki/Allosteric_regulation" title="Allosteric regulation">allosteric regulation</a>, often binding to these enzymes in a complex with <a href="/wiki/Calmodulin" title="Calmodulin">calmodulin</a>.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">&#91;</span>16<span class="cite-bracket">&#93;</span></a></sup> Calcium is, therefore, a <a href="/wiki/Cell_signaling" title="Cell signaling">cell signaling</a> molecule, and not usually considered a cofactor of the enzymes it regulates.<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">&#91;</span>17<span class="cite-bracket">&#93;</span></a></sup> </p><p>Other organisms require additional metals as enzyme cofactors, such as <a href="/wiki/Vanadium" title="Vanadium">vanadium</a> in the <a href="/wiki/Nitrogenase" title="Nitrogenase">nitrogenase</a> of the <a href="/wiki/Nitrogen_fixation" title="Nitrogen fixation">nitrogen-fixing</a> bacteria of the genus <i><a href="/wiki/Azotobacter" title="Azotobacter">Azotobacter</a></i>,<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">&#91;</span>18<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Tungsten" title="Tungsten">tungsten</a> in the <a href="/wiki/Aldehyde_ferredoxin_oxidoreductase" title="Aldehyde ferredoxin oxidoreductase">aldehyde ferredoxin oxidoreductase</a> of the thermophilic <a href="/wiki/Archaea" title="Archaea">archaean</a> <i><a href="/wiki/Pyrococcus_furiosus" title="Pyrococcus furiosus">Pyrococcus furiosus</a></i>,<sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">&#91;</span>19<span class="cite-bracket">&#93;</span></a></sup> and even <a href="/wiki/Cadmium" title="Cadmium">cadmium</a> in the <a href="/wiki/Carbonic_anhydrase" title="Carbonic anhydrase">carbonic anhydrase</a> from the marine <a href="/wiki/Diatom" title="Diatom">diatom</a> <i><a href="/wiki/Thalassiosira_weissflogii" title="Thalassiosira weissflogii">Thalassiosira weissflogii</a></i>.<sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">&#91;</span>20<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-21" class="reference"><a href="#cite_note-21"><span class="cite-bracket">&#91;</span>21<span class="cite-bracket">&#93;</span></a></sup> </p><p>In many cases, the cofactor includes both an inorganic and organic component. One diverse set of examples is the <a href="/wiki/Heme" title="Heme">heme</a> proteins, which consist of a <a href="/wiki/Porphyrin" title="Porphyrin">porphyrin</a> ring coordinated to <a href="/wiki/Iron" title="Iron">iron</a>.<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">&#91;</span>22<span class="cite-bracket">&#93;</span></a></sup> </p> <table class="wikitable" style="margin:auto; text-align:center;"> <tbody><tr> <th>Ion</th> <th>Examples of enzymes containing this ion </th></tr> <tr> <td><a href="/wiki/Copper#Biological_role" title="Copper">Cupric</a></td> <td><a href="/wiki/Cytochrome_oxidase" class="mw-redirect" title="Cytochrome oxidase">Cytochrome oxidase</a> </td></tr> <tr> <td><a href="/wiki/Iron" title="Iron">Ferrous or Ferric</a></td> <td><a href="/wiki/Catalase" title="Catalase">Catalase</a><br /><a href="/wiki/Cytochrome" title="Cytochrome">Cytochrome</a> (via <a href="/wiki/Heme" title="Heme">Heme</a>)<br /><a href="/wiki/Nitrogenase" title="Nitrogenase">Nitrogenase</a><br /><a href="/wiki/Hydrogenase" title="Hydrogenase">Hydrogenase</a> </td></tr> <tr> <td><a href="/wiki/Magnesium" title="Magnesium">Magnesium</a></td> <td><a href="/wiki/Glucose_6-phosphatase" title="Glucose 6-phosphatase">Glucose 6-phosphatase</a><br /><a href="/wiki/Hexokinase" title="Hexokinase">Hexokinase</a> <br /> <a href="/wiki/DNA_polymerase" title="DNA polymerase">DNA polymerase</a> </td></tr> <tr> <td><a href="/wiki/Manganese" title="Manganese">Manganese</a></td> <td><a href="/wiki/Arginase" title="Arginase">Arginase</a> </td></tr> <tr> <td><a href="/wiki/Molybdenum" title="Molybdenum">Molybdenum</a></td> <td><a href="/wiki/Nitrate_reductase" title="Nitrate reductase">Nitrate reductase</a><br /><a href="/wiki/Nitrogenase" title="Nitrogenase">Nitrogenase</a><br /><a href="/wiki/Xanthine_oxidase" title="Xanthine oxidase">Xanthine oxidase</a> </td></tr> <tr> <td><a href="/wiki/Nickel" title="Nickel">Nickel</a></td> <td><a href="/wiki/Urease" title="Urease">Urease</a> </td></tr> <tr> <td><a href="/wiki/Zinc" title="Zinc">Zinc</a></td> <td><a href="/wiki/Alcohol_dehydrogenase" title="Alcohol dehydrogenase">Alcohol dehydrogenase</a><br /><a href="/wiki/Carbonic_anhydrase" title="Carbonic anhydrase">Carbonic anhydrase</a><br /><a href="/wiki/DNA_polymerase" title="DNA polymerase">DNA polymerase</a> </td></tr></tbody></table> <figure class="mw-halign-right skin-invert-image" typeof="mw:File/Thumb"><a href="/wiki/File:2Fe2S.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/d/d9/2Fe2S.png/220px-2Fe2S.png" decoding="async" width="220" height="68" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/d9/2Fe2S.png/330px-2Fe2S.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/d9/2Fe2S.png/440px-2Fe2S.png 2x" data-file-width="711" data-file-height="220" /></a><figcaption>A simple [Fe<sub>2</sub>S<sub>2</sub>] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Iron–sulfur_clusters"><span id="Iron.E2.80.93sulfur_clusters"></span>Iron–sulfur clusters</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=4" title="Edit section: Iron–sulfur clusters"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Iron%E2%80%93sulfur_protein" title="Iron–sulfur protein">Iron–sulfur protein</a></div> <p>Iron–sulfur clusters are complexes of iron and sulfur atoms held within proteins by cysteinyl residues. They play both structural and functional roles, including electron transfer, redox sensing, and as structural modules.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">&#91;</span>23<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Organic">Organic</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=5" title="Edit section: Organic"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Organic cofactors are small organic molecules (typically a molecular mass less than 1000 Da) that can be either loosely or tightly bound to the enzyme and directly participate in the reaction.<sup id="cite_ref-Metzler_5-1" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">&#91;</span>24<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">&#91;</span>25<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-26" class="reference"><a href="#cite_note-26"><span class="cite-bracket">&#91;</span>26<span class="cite-bracket">&#93;</span></a></sup> In the latter case, when it is difficult to remove without denaturing the enzyme, it can be called a <a href="/wiki/Prosthetic_group" title="Prosthetic group">prosthetic group</a>. There is no sharp division between loosely and tightly bound cofactors.<sup id="cite_ref-Metzler_5-2" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup> Many such as NAD<sup>+</sup> can be tightly bound in some enzymes, while it is loosely bound in others.<sup id="cite_ref-Metzler_5-3" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup> Another example is <a href="/wiki/Thiamine_pyrophosphate" title="Thiamine pyrophosphate">thiamine pyrophosphate</a> (TPP), which is tightly bound in <a href="/wiki/Transketolase" title="Transketolase">transketolase</a> or <a href="/wiki/Pyruvate_decarboxylase" title="Pyruvate decarboxylase">pyruvate decarboxylase</a>, while it is less tightly bound in <a href="/wiki/Pyruvate_dehydrogenase" title="Pyruvate dehydrogenase">pyruvate dehydrogenase</a>.<sup id="cite_ref-27" class="reference"><a href="#cite_note-27"><span class="cite-bracket">&#91;</span>27<span class="cite-bracket">&#93;</span></a></sup> Other coenzymes, <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">flavin adenine dinucleotide</a> (FAD), <a href="/wiki/Biotin" title="Biotin">biotin</a>, and <a href="/wiki/Lipoamide" title="Lipoamide">lipoamide</a>, for instance, are tightly bound.<sup id="cite_ref-2017-Hanukoglu-JME_28-0" class="reference"><a href="#cite_note-2017-Hanukoglu-JME-28"><span class="cite-bracket">&#91;</span>28<span class="cite-bracket">&#93;</span></a></sup> Tightly bound cofactors are, in general, regenerated during the same reaction cycle, while loosely bound cofactors can be regenerated in a subsequent reaction catalyzed by a different enzyme. In the latter case, the cofactor can also be considered a substrate or cosubstrate. </p><p><a href="/wiki/Vitamin" title="Vitamin">Vitamins</a> can serve as precursors to many organic cofactors (e.g., vitamins <a href="/wiki/Vitamin_B1" class="mw-redirect" title="Vitamin B1">B<sub>1</sub></a>, <a href="/wiki/Vitamin_B2" class="mw-redirect" title="Vitamin B2">B<sub>2</sub></a>, <a href="/wiki/Vitamin_B6" title="Vitamin B6">B<sub>6</sub></a>, <a href="/wiki/Vitamin_B12" title="Vitamin B12">B<sub>12</sub></a>, <a href="/wiki/Niacin_(nutrient)" class="mw-redirect" title="Niacin (nutrient)">niacin</a>, <a href="/wiki/Folic_acid" class="mw-redirect" title="Folic acid">folic acid</a>) or as coenzymes themselves (e.g., <a href="/wiki/Vitamin_C" title="Vitamin C">vitamin C</a>). However, vitamins do have other functions in the body.<sup id="cite_ref-29" class="reference"><a href="#cite_note-29"><span class="cite-bracket">&#91;</span>29<span class="cite-bracket">&#93;</span></a></sup> Many organic cofactors also contain a <a href="/wiki/Nucleotide" title="Nucleotide">nucleotide</a>, such as the electron carriers <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NAD</a> and <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">FAD</a>, and <a href="/wiki/Coenzyme_A" title="Coenzyme A">coenzyme A</a>, which carries <a href="/wiki/Acyl" class="mw-redirect" title="Acyl">acyl</a> groups. Most of these cofactors are found in a huge variety of species, and some are universal to all forms of life. An exception to this wide distribution is a group of unique cofactors that evolved in <a href="/wiki/Methanogen" title="Methanogen">methanogens</a>, which are restricted to this group of <a href="/wiki/Archaea" title="Archaea">archaea</a>.<sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">&#91;</span>30<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Vitamins_and_derivatives">Vitamins and derivatives</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=6" title="Edit section: Vitamins and derivatives"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <table class="wikitable"> <tbody><tr> <th>Cofactor / Prosthetic group </th> <th>Vitamin</th> <th>Additional component</th> <th>Chemical group(s) transferred</th> <th>Distribution </th></tr> <tr> <td><a href="/wiki/Thiamine_pyrophosphate" title="Thiamine pyrophosphate">Thiamine pyrophosphate</a><sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">&#91;</span>31<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Thiamine" title="Thiamine">Thiamine</a> (B<sub>1</sub>)</td> <td><a href="/wiki/Pyrophosphate" title="Pyrophosphate">pyrophosphate</a></td> <td>2-carbon groups, α cleavage</td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NAD<sup>+</sup></a> and <a href="/wiki/Nicotinamide_adenine_dinucleotide_phosphate" title="Nicotinamide adenine dinucleotide phosphate">NADP<sup>+</sup></a><sup id="cite_ref-Pollak_32-0" class="reference"><a href="#cite_note-Pollak-32"><span class="cite-bracket">&#91;</span>32<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Niacin_(nutrient)" class="mw-redirect" title="Niacin (nutrient)">Niacin</a> (B<sub>3</sub>)</td> <td>ADP</td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Pyridoxal_phosphate" title="Pyridoxal phosphate">Pyridoxal phosphate</a><sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">&#91;</span>33<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Pyridoxine" title="Pyridoxine">Pyridoxine</a> (B<sub>6</sub>)</td> <td>None</td> <td>Amino and carboxyl groups</td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Methylcobalamin" title="Methylcobalamin">Methylcobalamin</a><sup id="cite_ref-34" class="reference"><a href="#cite_note-34"><span class="cite-bracket">&#91;</span>34<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Vitamin_B12" title="Vitamin B12">Vitamin B<sub>12</sub></a></td> <td>Methyl group</td> <td><a href="/wiki/Acyl" class="mw-redirect" title="Acyl">acyl groups</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Cobalamine" class="mw-redirect" title="Cobalamine">Cobalamine</a><sup id="cite_ref-Metzler_5-4" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Cobalamine" class="mw-redirect" title="Cobalamine">Cobalamine</a> (B<sub>12</sub>)</td> <td>None</td> <td><a href="/wiki/Hydrogen" title="Hydrogen">hydrogen</a>, <a href="/wiki/Alkyl" class="mw-redirect" title="Alkyl">alkyl groups</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Biotin" title="Biotin">Biotin</a><sup id="cite_ref-35" class="reference"><a href="#cite_note-35"><span class="cite-bracket">&#91;</span>35<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Biotin" title="Biotin">Biotin</a> (H)</td> <td>None</td> <td>CO<sub>2</sub></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Coenzyme_A" title="Coenzyme A">Coenzyme A</a><sup id="cite_ref-36" class="reference"><a href="#cite_note-36"><span class="cite-bracket">&#91;</span>36<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Pantothenic_acid" title="Pantothenic acid">Pantothenic acid</a> (B<sub>5</sub>)</td> <td>ADP</td> <td><a href="/wiki/Acetyl" class="mw-redirect" title="Acetyl">Acetyl group</a> and other <a href="/wiki/Acyl" class="mw-redirect" title="Acyl">acyl groups</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Tetrahydrofolic_acid" title="Tetrahydrofolic acid">Tetrahydrofolic acid</a><sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">&#91;</span>37<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Folic_acid" class="mw-redirect" title="Folic acid">Folic acid</a> (B<sub>9</sub>)</td> <td><a href="/wiki/Glutamic_acid" title="Glutamic acid">Glutamate</a> residues</td> <td><a href="/wiki/Methyl" class="mw-redirect" title="Methyl">Methyl</a>, <a href="/wiki/Aldehyde" title="Aldehyde">formyl</a>, <a href="/wiki/Methylene_group" title="Methylene group">methylene</a> and formimino groups</td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Vitamin_K" title="Vitamin K">Menaquinone</a><sup id="cite_ref-Søballe_38-0" class="reference"><a href="#cite_note-Søballe-38"><span class="cite-bracket">&#91;</span>38<span class="cite-bracket">&#93;</span></a></sup></td> <td>Vitamin K</td> <td>None</td> <td><a href="/wiki/Carbonyl" class="mw-redirect" title="Carbonyl">Carbonyl group</a> and <a href="/wiki/Electron" title="Electron">electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Ascorbic_acid" class="mw-redirect" title="Ascorbic acid">Ascorbic acid</a><sup id="cite_ref-39" class="reference"><a href="#cite_note-39"><span class="cite-bracket">&#91;</span>39<span class="cite-bracket">&#93;</span></a></sup></td> <td>Vitamin C</td> <td>None</td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Flavin_mononucleotide" title="Flavin mononucleotide">Flavin mononucleotide</a><sup id="cite_ref-Joosten_40-0" class="reference"><a href="#cite_note-Joosten-40"><span class="cite-bracket">&#91;</span>40<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Riboflavin" title="Riboflavin">Riboflavin</a> (B<sub>2</sub>)</td> <td>None</td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">Flavin adenine dinucleotide</a><sup id="cite_ref-Joosten_40-1" class="reference"><a href="#cite_note-Joosten-40"><span class="cite-bracket">&#91;</span>40<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Riboflavin" title="Riboflavin">Riboflavin</a> (B<sub>2</sub>)</td> <td>ADP</td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Coenzyme_F420" title="Coenzyme F420">Coenzyme F420</a><sup id="cite_ref-41" class="reference"><a href="#cite_note-41"><span class="cite-bracket">&#91;</span>41<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Riboflavin" title="Riboflavin">Riboflavin</a> (B<sub>2</sub>)</td> <td>Amino acids</td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Methanogen" title="Methanogen">Methanogens</a> and some <a href="/wiki/Bacteria" title="Bacteria">bacteria</a> </td></tr></tbody></table> <div class="mw-heading mw-heading3"><h3 id="Non-vitamins">Non-vitamins</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=7" title="Edit section: Non-vitamins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <table class="wikitable"> <tbody><tr> <th>Cofactor</th> <th>Chemical group(s) transferred</th> <th>Distribution </th></tr> <tr> <td><a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">Adenosine triphosphate</a><sup id="cite_ref-42" class="reference"><a href="#cite_note-42"><span class="cite-bracket">&#91;</span>42<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Phosphate" title="Phosphate">Phosphate group</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/S-Adenosyl_methionine" title="S-Adenosyl methionine">S-Adenosyl methionine</a><sup id="cite_ref-43" class="reference"><a href="#cite_note-43"><span class="cite-bracket">&#91;</span>43<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Methyl_group" title="Methyl group">Methyl group</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Coenzyme_B" title="Coenzyme B">Coenzyme B</a><sup id="cite_ref-44" class="reference"><a href="#cite_note-44"><span class="cite-bracket">&#91;</span>44<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Methanogen" title="Methanogen">Methanogens</a> </td></tr> <tr> <td><a href="/wiki/Coenzyme_M" title="Coenzyme M">Coenzyme M</a><sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">&#91;</span>45<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-46" class="reference"><a href="#cite_note-46"><span class="cite-bracket">&#91;</span>46<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Methyl_group" title="Methyl group">Methyl group</a></td> <td><a href="/wiki/Methanogen" title="Methanogen">Methanogens</a> </td></tr> <tr> <td><a href="/wiki/Coenzyme_Q" class="mw-redirect" title="Coenzyme Q">Coenzyme Q</a><sup id="cite_ref-47" class="reference"><a href="#cite_note-47"><span class="cite-bracket">&#91;</span>47<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Cytidine_triphosphate" title="Cytidine triphosphate">Cytidine triphosphate</a><sup id="cite_ref-Plantbiochemistry_48-0" class="reference"><a href="#cite_note-Plantbiochemistry-48"><span class="cite-bracket">&#91;</span>48<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Diacylglycerol" class="mw-redirect" title="Diacylglycerol">Diacylglycerols</a> and lipid head groups</td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Glutathione" title="Glutathione">Glutathione</a><sup id="cite_ref-49" class="reference"><a href="#cite_note-49"><span class="cite-bracket">&#91;</span>49<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-50" class="reference"><a href="#cite_note-50"><span class="cite-bracket">&#91;</span>50<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td>Some <a href="/wiki/Bacteria" title="Bacteria">bacteria</a> and most <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Heme" title="Heme">Heme</a><sup id="cite_ref-51" class="reference"><a href="#cite_note-51"><span class="cite-bracket">&#91;</span>51<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Lipoamide" title="Lipoamide">Lipoamide</a><sup id="cite_ref-Metzler_5-5" class="reference"><a href="#cite_note-Metzler-5"><span class="cite-bracket">&#91;</span>5<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electrons" class="mw-redirect" title="Electrons">Electrons</a>, <a href="/wiki/Acyl" class="mw-redirect" title="Acyl">acyl groups</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Methanofuran" title="Methanofuran">Methanofuran</a><sup id="cite_ref-52" class="reference"><a href="#cite_note-52"><span class="cite-bracket">&#91;</span>52<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Aldehyde" title="Aldehyde">Formyl group</a></td> <td><a href="/wiki/Methanogen" title="Methanogen">Methanogens</a> </td></tr> <tr> <td><a href="/wiki/Molybdopterin" title="Molybdopterin">Molybdopterin</a><sup id="cite_ref-53" class="reference"><a href="#cite_note-53"><span class="cite-bracket">&#91;</span>53<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-54" class="reference"><a href="#cite_note-54"><span class="cite-bracket">&#91;</span>54<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Oxygen" title="Oxygen">Oxygen</a> atoms</td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Nucleotide_sugar" title="Nucleotide sugar">Nucleotide sugars</a><sup id="cite_ref-Ginsburg_55-0" class="reference"><a href="#cite_note-Ginsburg-55"><span class="cite-bracket">&#91;</span>55<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Monosaccharide" title="Monosaccharide">Monosaccharides</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/3%27-Phosphoadenosine-5%27-phosphosulfate" title="3&#39;-Phosphoadenosine-5&#39;-phosphosulfate">3'-Phosphoadenosine-5'-phosphosulfate</a><sup id="cite_ref-56" class="reference"><a href="#cite_note-56"><span class="cite-bracket">&#91;</span>56<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Sulfate" title="Sulfate">Sulfate group</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Pyrroloquinoline_quinone" title="Pyrroloquinoline quinone">Pyrroloquinoline quinone</a><sup id="cite_ref-57" class="reference"><a href="#cite_note-57"><span class="cite-bracket">&#91;</span>57<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Electron" title="Electron">Electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a> </td></tr> <tr> <td><a href="/wiki/Tetrahydrobiopterin" title="Tetrahydrobiopterin">Tetrahydrobiopterin</a><sup id="cite_ref-58" class="reference"><a href="#cite_note-58"><span class="cite-bracket">&#91;</span>58<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Oxygen" title="Oxygen">Oxygen</a> atom and <a href="/wiki/Electron" title="Electron">electrons</a></td> <td><a href="/wiki/Bacteria" title="Bacteria">Bacteria</a>, <a href="/wiki/Archaea" title="Archaea">archaea</a> and <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a> </td></tr> <tr> <td><a href="/wiki/Tetrahydromethanopterin" title="Tetrahydromethanopterin">Tetrahydromethanopterin</a><sup id="cite_ref-59" class="reference"><a href="#cite_note-59"><span class="cite-bracket">&#91;</span>59<span class="cite-bracket">&#93;</span></a></sup></td> <td><a href="/wiki/Methyl_group" title="Methyl group">Methyl group</a></td> <td><a href="/wiki/Methanogen" title="Methanogen">Methanogens</a> </td></tr></tbody></table> <div class="mw-heading mw-heading3"><h3 id="Cofactors_as_metabolic_intermediates">Cofactors as metabolic intermediates</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=8" title="Edit section: Cofactors as metabolic intermediates"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right skin-invert-image" typeof="mw:File/Thumb"><a href="/wiki/File:NAD_oxidation_reduction.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/b5/NAD_oxidation_reduction.svg/250px-NAD_oxidation_reduction.svg.png" decoding="async" width="250" height="149" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/b5/NAD_oxidation_reduction.svg/375px-NAD_oxidation_reduction.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/b5/NAD_oxidation_reduction.svg/500px-NAD_oxidation_reduction.svg.png 2x" data-file-width="920" data-file-height="550" /></a><figcaption>The <a href="/wiki/Redox" title="Redox">redox</a> reactions of <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">nicotinamide adenine dinucleotide</a>.</figcaption></figure> <p>Metabolism involves a vast array of chemical reactions, but most fall under a few basic types of reactions that involve the transfer of <a href="/wiki/Functional_group" title="Functional group">functional groups</a>.<sup id="cite_ref-60" class="reference"><a href="#cite_note-60"><span class="cite-bracket">&#91;</span>60<span class="cite-bracket">&#93;</span></a></sup> This common chemistry allows cells to use a small set of metabolic intermediates to carry chemical groups between different reactions.<sup id="cite_ref-61" class="reference"><a href="#cite_note-61"><span class="cite-bracket">&#91;</span>61<span class="cite-bracket">&#93;</span></a></sup> These group-transfer intermediates are the loosely bound organic cofactors, often called <a href="/wiki/Enzyme#Coenzymes" title="Enzyme">coenzymes</a>. </p><p>Each class of group-transfer reaction is carried out by a particular cofactor, which is the substrate for a set of enzymes that produce it, and a set of enzymes that consume it. An example of this are the <a href="/wiki/Dehydrogenase" title="Dehydrogenase">dehydrogenases</a> that use <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">nicotinamide adenine dinucleotide</a> (NAD<sup>+</sup>) as a cofactor. Here, hundreds of separate types of enzymes remove electrons from their substrates and <a href="/wiki/Redox" title="Redox">reduce</a> NAD<sup>+</sup> to NADH. This reduced cofactor is then a substrate for any of the <a href="/wiki/Reductase" class="mw-redirect" title="Reductase">reductases</a> in the cell that require electrons to reduce their substrates.<sup id="cite_ref-Pollak_32-1" class="reference"><a href="#cite_note-Pollak-32"><span class="cite-bracket">&#91;</span>32<span class="cite-bracket">&#93;</span></a></sup> </p><p>Therefore, these cofactors are continuously recycled as part of <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>. As an example, the total quantity of ATP in the human body is about 0.1&#160;<a href="/wiki/Mole_(unit)" title="Mole (unit)">mole</a>. This ATP is constantly being broken down into ADP, and then converted back into ATP. Thus, at any given time, the total amount of ATP + ADP remains fairly constant. The energy used by human cells requires the <a href="/wiki/Hydrolysis" title="Hydrolysis">hydrolysis</a> of 100 to 150&#160;moles of ATP daily, which is around 50 to 75&#160;kg. In typical situations, humans use up their body weight of ATP over the course of the day.<sup id="cite_ref-Di_Carlo_62-0" class="reference"><a href="#cite_note-Di_Carlo-62"><span class="cite-bracket">&#91;</span>62<span class="cite-bracket">&#93;</span></a></sup> This means that each ATP molecule is recycled 1000 to 1500 times daily. </p> <div class="mw-heading mw-heading3"><h3 id="Evolution">Evolution</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=9" title="Edit section: Evolution"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Abiogenesis" title="Abiogenesis">Abiogenesis</a></div> <p>Organic cofactors, such as <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a> and <a href="/wiki/NADH" class="mw-redirect" title="NADH">NADH</a>, are present in all known forms of life and form a core part of <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>. Such universal <a href="/wiki/Conservation_(genetics)" class="mw-redirect" title="Conservation (genetics)">conservation</a> indicates that these molecules evolved very early in the development of living things.<sup id="cite_ref-63" class="reference"><a href="#cite_note-63"><span class="cite-bracket">&#91;</span>63<span class="cite-bracket">&#93;</span></a></sup> At least some of the current set of cofactors may, therefore, have been present in the <a href="/wiki/Last_universal_ancestor" class="mw-redirect" title="Last universal ancestor">last universal ancestor</a>, which lived about 4 billion years ago.<sup id="cite_ref-64" class="reference"><a href="#cite_note-64"><span class="cite-bracket">&#91;</span>64<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-65" class="reference"><a href="#cite_note-65"><span class="cite-bracket">&#91;</span>65<span class="cite-bracket">&#93;</span></a></sup> </p><p>Organic cofactors may have been present even earlier in the <a href="/wiki/Timeline_of_evolution" class="mw-redirect" title="Timeline of evolution">history of life</a> on Earth.<sup id="cite_ref-66" class="reference"><a href="#cite_note-66"><span class="cite-bracket">&#91;</span>66<span class="cite-bracket">&#93;</span></a></sup> The nucleotide <a href="/wiki/Adenosine" title="Adenosine">adenosine</a> is a cofactor for many basic metabolic enzymes such as transferases. It may be a remnant of the <a href="/wiki/RNA_world_hypothesis" class="mw-redirect" title="RNA world hypothesis">RNA world</a>.<sup id="cite_ref-67" class="reference"><a href="#cite_note-67"><span class="cite-bracket">&#91;</span>67<span class="cite-bracket">&#93;</span></a></sup><sup id="cite_ref-68" class="reference"><a href="#cite_note-68"><span class="cite-bracket">&#91;</span>68<span class="cite-bracket">&#93;</span></a></sup> Adenosine-based cofactors may have acted as adaptors that allowed enzymes and ribozymes to bind new cofactors through small modifications in existing adenosine-binding <a href="/wiki/Protein_domain" title="Protein domain">domains</a>, which had originally evolved to bind a different cofactor.<sup id="cite_ref-Denessiouk_9-1" class="reference"><a href="#cite_note-Denessiouk-9"><span class="cite-bracket">&#91;</span>9<span class="cite-bracket">&#93;</span></a></sup> This process of adapting a pre-evolved structure for a novel use is known as <i><a href="/wiki/Exaptation" title="Exaptation">exaptation</a></i>. </p><p><b>Prebiotic origin of coenzymes</b>. Like <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> and <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a>, certain <a href="/wiki/Vitamin" title="Vitamin">vitamins</a> and thus coenzymes can be created under early earth conditions. For instance, <a href="/wiki/Vitamin_B3" title="Vitamin B3">vitamin B3</a> can be synthesized with electric discharges applied to <a href="/wiki/Ethylene" title="Ethylene">ethylene</a> and <a href="/wiki/Ammonia" title="Ammonia">ammonia</a>.<sup id="cite_ref-69" class="reference"><a href="#cite_note-69"><span class="cite-bracket">&#91;</span>69<span class="cite-bracket">&#93;</span></a></sup> Similarly, <a href="/wiki/Pantetheine" title="Pantetheine">pantetheine</a> (a <a href="/wiki/Pantothenic_acid" title="Pantothenic acid">vitamin B5</a> derivative), a precursor of <a href="/wiki/Coenzyme_A" title="Coenzyme A">coenzyme A</a> and thioester-dependent synthesis, can be formed spontaneously under evaporative conditions.<sup id="cite_ref-70" class="reference"><a href="#cite_note-70"><span class="cite-bracket">&#91;</span>70<span class="cite-bracket">&#93;</span></a></sup> Other coenzymes may have existed early on Earth, such as <a href="/wiki/Pterin" title="Pterin">pterins</a> (a derivative of <a href="/wiki/Folate" title="Folate">vitamin B9</a>), <a href="/wiki/Flavin_group" title="Flavin group">flavins</a> (<a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">FAD</a>, <a href="/wiki/Flavin_mononucleotide" title="Flavin mononucleotide">flavin mononucleotide</a> = FMN), and <a href="/wiki/Riboflavin" title="Riboflavin">riboflavin</a> (vitamin B2).<sup id="cite_ref-71" class="reference"><a href="#cite_note-71"><span class="cite-bracket">&#91;</span>71<span class="cite-bracket">&#93;</span></a></sup> </p><p><b>Changes in coenzymes</b>. A computational method, IPRO, recently predicted mutations that experimentally switched the cofactor specificity of <i>Candida boidinii</i> xylose reductase from NADPH to NADH.<sup id="cite_ref-72" class="reference"><a href="#cite_note-72"><span class="cite-bracket">&#91;</span>72<span class="cite-bracket">&#93;</span></a></sup> </p><p><b>Evolution of enzymes without coenzymes</b>. If enzymes require a co-enzyme, how does the coenzyme evolve? The most likely scenario is that enzymes can function initially without their coenzymes and later recruit the coenzyme, even if the catalyzed reaction may not be as efficient or as fast. Examples are <a href="/wiki/Alcohol_dehydrogenase" title="Alcohol dehydrogenase">Alcohol Dehydrogenase</a> (coenzyme: <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NAD⁺</a>),<sup id="cite_ref-73" class="reference"><a href="#cite_note-73"><span class="cite-bracket">&#91;</span>73<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Lactate_dehydrogenase" title="Lactate dehydrogenase">Lactate Dehydrogenase</a> (NAD⁺),<sup id="cite_ref-74" class="reference"><a href="#cite_note-74"><span class="cite-bracket">&#91;</span>74<span class="cite-bracket">&#93;</span></a></sup> <a href="/wiki/Glutathione_reductase" title="Glutathione reductase">Glutathione Reductase</a> (<a href="/wiki/Nicotinamide_adenine_dinucleotide_phosphate" title="Nicotinamide adenine dinucleotide phosphate">NADPH</a>).<sup id="cite_ref-75" class="reference"><a href="#cite_note-75"><span class="cite-bracket">&#91;</span>75<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="History">History</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=10" title="Edit section: History"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/History_of_biochemistry" title="History of biochemistry">History of biochemistry</a></div> <p>The first organic cofactor to be discovered was NAD<sup>+</sup>, which was identified by <a href="/wiki/Arthur_Harden" title="Arthur Harden">Arthur Harden</a> and William Young 1906.<sup id="cite_ref-76" class="reference"><a href="#cite_note-76"><span class="cite-bracket">&#91;</span>76<span class="cite-bracket">&#93;</span></a></sup> They noticed that adding boiled and filtered <a href="/wiki/Yeast" title="Yeast">yeast</a> extract greatly accelerated <a href="/wiki/Alcoholic_fermentation" class="mw-redirect" title="Alcoholic fermentation">alcoholic fermentation</a> in unboiled yeast extracts. They called the unidentified factor responsible for this effect a <i>coferment</i>. Through a long and difficult purification from yeast extracts, this heat-stable factor was identified as a <a href="/wiki/Nucleotide" title="Nucleotide">nucleotide</a> sugar phosphate by <a href="/wiki/Hans_von_Euler-Chelpin" title="Hans von Euler-Chelpin">Hans von Euler-Chelpin</a>.<sup id="cite_ref-77" class="reference"><a href="#cite_note-77"><span class="cite-bracket">&#91;</span>77<span class="cite-bracket">&#93;</span></a></sup> Other cofactors were identified throughout the early 20th century, with ATP being isolated in 1929 by Karl Lohmann,<sup id="cite_ref-78" class="reference"><a href="#cite_note-78"><span class="cite-bracket">&#91;</span>78<span class="cite-bracket">&#93;</span></a></sup> and coenzyme A being discovered in 1945 by <a href="/wiki/Fritz_Albert_Lipmann" title="Fritz Albert Lipmann">Fritz Albert Lipmann</a>.<sup id="cite_ref-79" class="reference"><a href="#cite_note-79"><span class="cite-bracket">&#91;</span>79<span class="cite-bracket">&#93;</span></a></sup> </p><p>The functions of these molecules were at first mysterious, but, in 1936, <a href="/wiki/Otto_Heinrich_Warburg" title="Otto Heinrich Warburg">Otto Heinrich Warburg</a> identified the function of NAD<sup>+</sup> in hydride transfer.<sup id="cite_ref-80" class="reference"><a href="#cite_note-80"><span class="cite-bracket">&#91;</span>80<span class="cite-bracket">&#93;</span></a></sup> This discovery was followed in the early 1940s by the work of <a href="/wiki/Herman_Kalckar" title="Herman Kalckar">Herman Kalckar</a>, who established the link between the oxidation of sugars and the generation of ATP.<sup id="cite_ref-81" class="reference"><a href="#cite_note-81"><span class="cite-bracket">&#91;</span>81<span class="cite-bracket">&#93;</span></a></sup> This confirmed the central role of ATP in energy transfer that had been proposed by Fritz Albert Lipmann in 1941.<sup id="cite_ref-82" class="reference"><a href="#cite_note-82"><span class="cite-bracket">&#91;</span>82<span class="cite-bracket">&#93;</span></a></sup> Later, in 1949, Morris Friedkin and <a href="/wiki/Albert_L._Lehninger" title="Albert L. Lehninger">Albert L. Lehninger</a> proved that NAD<sup>+</sup> linked metabolic pathways such as the citric acid cycle and the synthesis of ATP.<sup id="cite_ref-83" class="reference"><a href="#cite_note-83"><span class="cite-bracket">&#91;</span>83<span class="cite-bracket">&#93;</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Protein-derived_cofactors">Protein-derived cofactors</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=11" title="Edit section: Protein-derived cofactors"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In a number of enzymes, the moiety that acts as a cofactor is formed by post-translational modification of a part of the protein sequence. This often replaces the need for an external binding factor, such as a metal ion, for protein function. Potential modifications could be oxidation of aromatic residues, binding between residues, cleavage or ring-forming.<sup id="cite_ref-Davidson_5283–5292_84-0" class="reference"><a href="#cite_note-Davidson_5283–5292-84"><span class="cite-bracket">&#91;</span>84<span class="cite-bracket">&#93;</span></a></sup> These alterations are distinct from other <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translation protein modifications</a>, such as <a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a>, <a href="/wiki/Methylation" title="Methylation">methylation</a>, or <a href="/wiki/Glycosylation" title="Glycosylation">glycosylation</a> in that the amino acids typically acquire new functions. This increases the functionality of the protein; unmodified amino acids are typically limited to acid-base reactions, and the alteration of resides can give the protein electrophilic sites or the ability to stabilize free radicals.<sup id="cite_ref-Davidson_5283–5292_84-1" class="reference"><a href="#cite_note-Davidson_5283–5292-84"><span class="cite-bracket">&#91;</span>84<span class="cite-bracket">&#93;</span></a></sup> Examples of cofactor production include <a href="/wiki/Tryptophan_tryptophylquinone" title="Tryptophan tryptophylquinone">tryptophan tryptophylquinone</a> (TTQ), derived from two tryptophan side chains,<sup id="cite_ref-85" class="reference"><a href="#cite_note-85"><span class="cite-bracket">&#91;</span>85<span class="cite-bracket">&#93;</span></a></sup> and 4-methylidene-imidazole-5-one (MIO), derived from an Ala-Ser-Gly motif.<sup id="cite_ref-86" class="reference"><a href="#cite_note-86"><span class="cite-bracket">&#91;</span>86<span class="cite-bracket">&#93;</span></a></sup> Characterization of protein-derived cofactors is conducted using <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">X-ray crystallography</a> and <a href="/wiki/Mass_spectrometry" title="Mass spectrometry">mass spectroscopy</a>; structural data is necessary because sequencing does not readily identify the altered sites. </p> <div class="mw-heading mw-heading2"><h2 id="Non-enzymatic_cofactors">Non-enzymatic cofactors</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=12" title="Edit section: Non-enzymatic cofactors"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The term is used in other areas of biology to refer more broadly to non-protein (or even protein) molecules that either activate, inhibit, or are required for the protein to function. For example, <a href="/wiki/Ligand_(biochemistry)" title="Ligand (biochemistry)">ligands</a> such as <a href="/wiki/Hormones" class="mw-redirect" title="Hormones">hormones</a> that bind to and activate <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">receptor proteins</a> are termed cofactors or coactivators, whereas molecules that inhibit receptor proteins are termed corepressors. One such example is the G protein-coupled receptor family of receptors, which are frequently found in sensory neurons. Ligand binding to the receptors activates the G protein, which then activates an enzyme to activate the effector.<sup id="cite_ref-87" class="reference"><a href="#cite_note-87"><span class="cite-bracket">&#91;</span>87<span class="cite-bracket">&#93;</span></a></sup> In order to avoid confusion, it has been suggested that such proteins that have ligand-binding mediated activation or repression be referred to as coregulators.<sup id="cite_ref-88" class="reference"><a href="#cite_note-88"><span class="cite-bracket">&#91;</span>88<span class="cite-bracket">&#93;</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=Cofactor_(biochemistry)&amp;action=edit&amp;section=13" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li> <li><a href="/wiki/Inorganic_chemistry" title="Inorganic chemistry">Inorganic chemistry</a></li> <li><a href="/wiki/Organometallic_chemistry" title="Organometallic chemistry">Organometallic chemistry</a></li> <li><a href="/wiki/Bioorganometallic_chemistry" title="Bioorganometallic chemistry">Bioorganometallic chemistry</a></li> <li><a href="/wiki/Cofactor_engineering" title="Cofactor engineering">Cofactor engineering</a></li></ul> <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=Cofactor_(biochemistry)&amp;action=edit&amp;section=14" 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 reflist-columns references-column-width" style="column-width: 30em;"> <ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</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="CITEREFHasimAdnan2010" class="citation journal cs1">Hasim, Onn H.; Adnan, Nor Azila (2010). <a rel="nofollow" class="external text" href="http://eprints.um.edu.my/3450/1/Coenzyme%2C_cofactor_and_prosthetic_group%C3%A2%E2%82%AC%E2%80%9Dambiguous_biochemical_jargon.pdf">"Coenzyme, Cofactor and Prosthetic Group — Ambiguous Biochemical Jargon"</a> <span class="cs1-format">(PDF)</span>. <i>Biochemical Education</i>. <b>22</b> (2): 93–94. <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%2F0307-4412%2894%2990088-4">10.1016/0307-4412(94)90088-4</a>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rft.genre=article&amp;rft.jtitle=Biochemical+Education&amp;rft.atitle=Coenzyme%2C+Cofactor+and+Prosthetic+Group+%E2%80%94+Ambiguous+Biochemical+Jargon&amp;rft.volume=22&amp;rft.issue=2&amp;rft.pages=93-94&amp;rft.date=2010&amp;rft_id=info%3Adoi%2F10.1016%2F0307-4412%2894%2990088-4&amp;rft.aulast=Hasim&amp;rft.aufirst=Onn+H.&amp;rft.au=Adnan%2C+Nor+Azila&amp;rft_id=http%3A%2F%2Feprints.um.edu.my%2F3450%2F1%2FCoenzyme%252C_cofactor_and_prosthetic_group%25C3%25A2%25E2%2582%25AC%25E2%2580%259Dambiguous_biochemical_jargon.pdf&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-2"><span class="mw-cite-backlink"><b><a href="#cite_ref-2">^</a></b></span> <span class="reference-text"><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/19990826022727/http://academic.brooklyn.cuny.edu/biology/bio4fv/page/coenzy_.htm">"Coenzymes and cofactors"</a>. Archived from <a rel="nofollow" class="external text" href="http://academic.brooklyn.cuny.edu/biology/bio4fv/page/coenzy_.htm">the original</a> on 1999-08-26<span class="reference-accessdate">. Retrieved <span class="nowrap">2007-11-17</span></span>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&amp;rft.genre=unknown&amp;rft.btitle=Coenzymes+and+cofactors&amp;rft_id=http%3A%2F%2Facademic.brooklyn.cuny.edu%2Fbiology%2Fbio4fv%2Fpage%2Fcoenzy_.htm&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-3"><span class="mw-cite-backlink"><b><a href="#cite_ref-3">^</a></b></span> <span class="reference-text"><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/20030505032408/http://www.elmhurst.edu/~chm/vchembook/571cofactor.html">"Enzyme Cofactors"</a>. Archived from <a rel="nofollow" class="external text" href="http://www.elmhurst.edu/~chm/vchembook/571cofactor.html">the original</a> on 2003-05-05<span class="reference-accessdate">. Retrieved <span class="nowrap">2007-11-17</span></span>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&amp;rft.genre=unknown&amp;rft.btitle=Enzyme+Cofactors&amp;rft_id=http%3A%2F%2Fwww.elmhurst.edu%2F~chm%2Fvchembook%2F571cofactor.html&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-4"><span class="mw-cite-backlink"><b><a href="#cite_ref-4">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFNelsonCox2008" class="citation book cs1">Nelson DL, Cox MM (2008). <i>Lehninger Principles of Biochemistry</i> (Fifth&#160;ed.). New York: W.H. 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title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rft.genre=article&amp;rft.jtitle=Annual+Review+of+Biochemistry&amp;rft.atitle=Posttranslational+biosynthesis+of+the+protein-derived+cofactor+tryptophan+tryptophylquinone&amp;rft.volume=82&amp;rft.pages=531-50&amp;rft.date=2013&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4082410%23id-name%3DPMC&amp;rft_id=info%3Apmid%2F23746262&amp;rft_id=info%3Adoi%2F10.1146%2Fannurev-biochem-051110-133601&amp;rft.aulast=Davidson&amp;rft.aufirst=VL&amp;rft.au=Wilmot%2C+CM&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4082410&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-86"><span class="mw-cite-backlink"><b><a href="#cite_ref-86">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHuangLohmanHuangShen2013" class="citation journal cs1">Huang SX, Lohman JR, Huang T, Shen B (May 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3657804">"A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. <b>110</b> (20): 8069–74. <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/2013PNAS..110.8069H">2013PNAS..110.8069H</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.1304733110">10.1073/pnas.1304733110</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&#160;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3657804">3657804</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&#160;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23633564">23633564</a>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rft.genre=article&amp;rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+of+the+United+States+of+America&amp;rft.atitle=A+new+member+of+the+4-methylideneimidazole-5-one-containing+aminomutase+family+from+the+enediyne+kedarcidin+biosynthetic+pathway&amp;rft.volume=110&amp;rft.issue=20&amp;rft.pages=8069-74&amp;rft.date=2013-05&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3657804%23id-name%3DPMC&amp;rft_id=info%3Apmid%2F23633564&amp;rft_id=info%3Adoi%2F10.1073%2Fpnas.1304733110&amp;rft_id=info%3Abibcode%2F2013PNAS..110.8069H&amp;rft.aulast=Huang&amp;rft.aufirst=SX&amp;rft.au=Lohman%2C+JR&amp;rft.au=Huang%2C+T&amp;rft.au=Shen%2C+B&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3657804&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-87"><span class="mw-cite-backlink"><b><a href="#cite_ref-87">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLodishBerkZipurskyMatsudaira2000" class="citation book cs1">Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James (2000-01-01). "G Protein–Coupled Receptors and Their Effectors". <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK21718/"><i>Molecular Cell Biology</i></a> (4th&#160;ed.).</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&amp;rft.genre=bookitem&amp;rft.atitle=G+Protein%E2%80%93Coupled+Receptors+and+Their+Effectors&amp;rft.btitle=Molecular+Cell+Biology&amp;rft.edition=4th&amp;rft.date=2000-01-01&amp;rft.aulast=Lodish&amp;rft.aufirst=Harvey&amp;rft.au=Berk%2C+Arnold&amp;rft.au=Zipursky%2C+S.+Lawrence&amp;rft.au=Matsudaira%2C+Paul&amp;rft.au=Baltimore%2C+David&amp;rft.au=Darnell%2C+James&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK21718%2F&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> <li id="cite_note-88"><span class="mw-cite-backlink"><b><a href="#cite_ref-88">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFO&#39;MalleyMcKenna2008" class="citation journal cs1">O'Malley BW, McKenna NJ (October 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582534">"Coactivators and corepressors: what's in a name?"</a>. <i>Molecular Endocrinology</i>. <b>22</b> (10): 2213–4. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1210%2Fme.2008-0201">10.1210/me.2008-0201</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a>&#160;<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2582534">2582534</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a>&#160;<a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18701638">18701638</a>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&amp;rft.genre=article&amp;rft.jtitle=Molecular+Endocrinology&amp;rft.atitle=Coactivators+and+corepressors%3A+what%27s+in+a+name%3F&amp;rft.volume=22&amp;rft.issue=10&amp;rft.pages=2213-4&amp;rft.date=2008-10&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2582534%23id-name%3DPMC&amp;rft_id=info%3Apmid%2F18701638&amp;rft_id=info%3Adoi%2F10.1210%2Fme.2008-0201&amp;rft.aulast=O%27Malley&amp;rft.aufirst=BW&amp;rft.au=McKenna%2C+NJ&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2582534&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></span> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Cofactor_(biochemistry)&amp;action=edit&amp;section=15" title="Edit section: Further reading"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFBugg1997" class="citation book cs1">Bugg T (1997). <span class="id-lock-registration" title="Free registration required"><a rel="nofollow" class="external text" href="https://archive.org/details/introductiontoen0000bugg"><i>An introduction to enzyme and coenzyme chemistry</i></a></span>. Oxford: Blackwell Science. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a>&#160;<a href="/wiki/Special:BookSources/978-0-86542-793-8" title="Special:BookSources/978-0-86542-793-8"><bdi>978-0-86542-793-8</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&amp;rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&amp;rft.genre=book&amp;rft.btitle=An+introduction+to+enzyme+and+coenzyme+chemistry&amp;rft.place=Oxford&amp;rft.pub=Blackwell+Science&amp;rft.date=1997&amp;rft.isbn=978-0-86542-793-8&amp;rft.aulast=Bugg&amp;rft.aufirst=Tim&amp;rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fintroductiontoen0000bugg&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3ACofactor+%28biochemistry%29" class="Z3988"></span></li></ul> <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=Cofactor_(biochemistry)&amp;action=edit&amp;section=16" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="http://www.bio.mtu.edu/%7Ehlyoungs/BL4010/cofactors.ppt">Cofactors lecture</a> <a rel="nofollow" class="external text" href="https://web.archive.org/web/20161005230343/http://www.bio.mtu.edu/%7Ehlyoungs/BL4010/cofactors.ppt">Archived</a> 2016-10-05 at the <a href="/wiki/Wayback_Machine" title="Wayback Machine">Wayback Machine</a> (Powerpoint file)</li> <li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Enzyme+cofactors">Enzyme+cofactors</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> <li><a rel="nofollow" class="external text" href="http://www.ebi.ac.uk/thornton-srv/databases/CoFactor/">The CoFactor Database</a></li></ul> <div class="navbox-styles"><style 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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 class="mw-selflink selflink">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 href="/wiki/Translocase" title="Translocase">Translocases</a></b> (<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"></div><div role="navigation" class="navbox" aria-labelledby="Enzyme_cofactors" 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:Enzyme_cofactors" title="Template:Enzyme cofactors"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzyme_cofactors" title="Template talk:Enzyme cofactors"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzyme_cofactors" title="Special:EditPage/Template:Enzyme cofactors"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzyme_cofactors" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzyme</a> <a class="mw-selflink selflink">cofactors</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Active forms</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/Vitamin" title="Vitamin">vitamins</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/Thiamine_pyrophosphate" title="Thiamine pyrophosphate">TPP / ThDP</a> (B<sub>1</sub>)</li> <li><a href="/wiki/Flavin_mononucleotide" title="Flavin mononucleotide">FMN</a>, <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">FAD</a> (B<sub>2</sub>)</li> <li><a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NAD<sup>+</sup></a>, <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">NADH</a>, <a href="/wiki/Nicotinamide_adenine_dinucleotide_phosphate" title="Nicotinamide adenine dinucleotide phosphate">NADP<sup>+</sup></a>, <a href="/wiki/Nicotinamide_adenine_dinucleotide_phosphate" title="Nicotinamide adenine dinucleotide phosphate">NADPH</a> (B<sub>3</sub>)</li> <li><a href="/wiki/Coenzyme_A" title="Coenzyme A">Coenzyme A</a> (B<sub>5</sub>)</li> <li><a href="/wiki/Pyridoxal_phosphate" title="Pyridoxal phosphate">PLP / P5P</a> (B<sub>6</sub>)</li> <li><a href="/wiki/Biotin" title="Biotin">Biotin</a> (B<sub>7</sub>)</li> <li><a href="/wiki/Tetrahydrofolic_acid" title="Tetrahydrofolic acid">THFA / H<sub>4</sub>FA</a>, <a href="/wiki/Dihydrofolic_acid" title="Dihydrofolic acid">DHFA / H<sub>2</sub>FA</a>, <a href="/wiki/5,10-Methylenetetrahydrofolate" title="5,10-Methylenetetrahydrofolate">MTHF</a> (B<sub>9</sub>)</li> <li><a href="/wiki/Adenosylcobalamin" title="Adenosylcobalamin">AdoCbl</a>, <a href="/wiki/Methylcobalamin" title="Methylcobalamin">MeCbl</a> (B<sub>12</sub>)</li> <li><a href="/wiki/Vitamin_C" title="Vitamin C">Ascorbic acid</a> (C)</li> <li><a href="/wiki/Phytomenadione" title="Phytomenadione">Phylloquinone</a> (K<sub>1</sub>), <a href="/wiki/Vitamin_K" title="Vitamin K">Menaquinone</a> (K<sub>2</sub>)</li> <li><a href="/wiki/Coenzyme_F420" title="Coenzyme F420">Coenzyme F420</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a class="mw-selflink-fragment" href="#Non-vitamins">non-vitamins</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/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a></li> <li><a href="/wiki/Cytidine_triphosphate" title="Cytidine triphosphate">CTP</a></li> <li><a href="/wiki/S-Adenosyl_methionine" title="S-Adenosyl methionine">SAMe</a></li> <li><a href="/wiki/3%27-Phosphoadenosine-5%27-phosphosulfate" title="3&#39;-Phosphoadenosine-5&#39;-phosphosulfate">PAPS</a></li> <li><a href="/wiki/Glutathione" title="Glutathione">GSH</a></li> <li><a href="/wiki/Coenzyme_B" title="Coenzyme B">Coenzyme B</a></li> <li><a href="/wiki/Cofactor_F430" title="Cofactor F430">Cofactor F430</a></li> <li><a href="/wiki/Coenzyme_M" title="Coenzyme M">Coenzyme M</a></li> <li><a href="/wiki/Coenzyme_Q10" title="Coenzyme Q10">Coenzyme Q</a></li> <li><a href="/wiki/Heme" title="Heme">Heme / Haem</a> (<a href="/wiki/Heme_A" title="Heme A">A</a>, <a href="/wiki/Heme_B" title="Heme B">B</a>, <a href="/wiki/Heme_C" title="Heme C">C</a>, <a href="/wiki/Heme_O" title="Heme O">O</a>)</li> <li><a href="/wiki/Lipoic_acid" title="Lipoic acid">Lipoic Acid</a></li> <li><a href="/wiki/Methanofuran" title="Methanofuran">Methanofuran</a></li> <li><a href="/wiki/Molybdopterin" title="Molybdopterin">Molybdopterin</a></li> <li><a href="/wiki/Mycofactocin" title="Mycofactocin">Mycofactocin</a></li> <li><a href="/wiki/Pyrroloquinoline_quinone" title="Pyrroloquinoline quinone">PQQ</a></li> <li><a href="/wiki/Tetrahydrobiopterin" title="Tetrahydrobiopterin">THB / BH<sub>4</sub></a></li> <li><a href="/wiki/Tetrahydromethanopterin" title="Tetrahydromethanopterin">THMPT / H<sub>4</sub>MPT</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Mineral_(nutrient)" title="Mineral (nutrient)">metal ions</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/Calcium" title="Calcium">Ca<sup>2+</sup></a></li> <li><a href="/wiki/Copper" title="Copper">Cu<sup>2+</sup></a></li> <li><a href="/wiki/Iron" title="Iron">Fe<sup>2+</sup>, Fe<sup>3+</sup></a></li> <li><a href="/wiki/Magnesium" title="Magnesium">Mg<sup>2+</sup></a></li> <li><a href="/wiki/Manganese" title="Manganese">Mn<sup>2+</sup></a></li> <li><a href="/wiki/Molybdenum" title="Molybdenum">Mo</a></li> <li><a href="/wiki/Nickel" title="Nickel">Ni<sup>2+</sup></a></li> <li><a href="/wiki/Zinc" title="Zinc">Zn<sup>2+</sup></a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Base forms</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><a href="/wiki/Vitamin" title="Vitamin">vitamins</a></i>: <i>see <a href="/wiki/Template:Vitamins" 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