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Oxyanion hole - Wikipedia

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href="https://es.wikipedia.org/wiki/Agujero_de_oxiani%C3%B3n" title="Agujero de oxianión – Spanish" lang="es" hreflang="es" data-title="Agujero de oxianión" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Trou_oxyanion" title="Trou oxyanion – French" lang="fr" hreflang="fr" data-title="Trou oxyanion" 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/Burato_de_oxiani%C3%B3n" title="Burato de oxianión – Galician" lang="gl" hreflang="gl" data-title="Burato de oxianión" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-ko 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</div> </div> </div> </div> </div> </div> </nav> </div> </div> </div> <div class="vector-column-end"> <div class="vector-sticky-pinned-container"> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-pinned-container" class="vector-pinned-container"> </div> </nav> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-pinned-container" class="vector-pinned-container"> <div id="vector-appearance" class="vector-appearance vector-pinnable-element"> <div class="vector-pinnable-header vector-appearance-pinnable-header vector-pinnable-header-pinned" data-feature-name="appearance-pinned" data-pinnable-element-id="vector-appearance" data-pinned-container-id="vector-appearance-pinned-container" data-unpinned-container-id="vector-appearance-unpinned-container" > <div class="vector-pinnable-header-label">Appearance</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-appearance.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-appearance.unpin">hide</button> </div> </div> </div> </nav> </div> </div> <div id="bodyContent" class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Pocket in the active site of an enzyme</div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Serine_protease_oxyanion_hole.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Serine_protease_oxyanion_hole.png/220px-Serine_protease_oxyanion_hole.png" decoding="async" width="220" height="138" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Serine_protease_oxyanion_hole.png/330px-Serine_protease_oxyanion_hole.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/ff/Serine_protease_oxyanion_hole.png/440px-Serine_protease_oxyanion_hole.png 2x" data-file-width="730" data-file-height="458" /></a><figcaption>Oxyanion hole of a <a href="/wiki/Serine_protease" title="Serine protease">serine protease</a> (black) stabilises negative charge build-up on the <a href="/wiki/Transition_state" title="Transition state">transition state</a> of the substrate (red) using hydrogen bonds from enzyme's <a href="/wiki/Peptide" title="Peptide">backbone</a> amides (blue).</figcaption></figure> <p>An <b>oxyanion hole</b> is a pocket in the <a href="/wiki/Active_site" title="Active site">active site</a> of an <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> that stabilizes <a href="/wiki/Transition_state" title="Transition state">transition state</a> negative charge on a <a href="/wiki/Deprotonation" title="Deprotonation">deprotonated</a> <a href="/wiki/Oxygen" title="Oxygen">oxygen</a> or <a href="/wiki/Alkoxide" title="Alkoxide">alkoxide</a>.<sup id="cite_ref-Stryer_Ch9_1-0" class="reference"><a href="#cite_note-Stryer_Ch9-1"><span class="cite-bracket">&#91;</span>1<span class="cite-bracket">&#93;</span></a></sup> The pocket typically consists of backbone amides or positively charged residues. Stabilising the transition state lowers the <a href="/wiki/Activation_energy" title="Activation energy">activation energy</a> necessary for the reaction, and so promotes <a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">catalysis</a>.<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> For example, <a href="/wiki/Protease" title="Protease">proteases</a> such as <a href="/wiki/Chymotrypsin" title="Chymotrypsin">chymotrypsin</a> contain an oxyanion hole to stabilise the <a href="/wiki/Tetrahedral_molecular_geometry" title="Tetrahedral molecular geometry">tetrahedral intermediate</a> anion formed during <a href="/wiki/Proteolytic" class="mw-redirect" title="Proteolytic">proteolysis</a> and protects <a href="/wiki/Substrate_(chemistry)" title="Substrate (chemistry)">substrate</a>'s negatively charged oxygen from <a href="/wiki/Water" title="Water">water</a> molecules.<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> Additionally, it may allow for insertion or positioning of a substrate, which would suffer from <a href="/wiki/Steric_hindrance" class="mw-redirect" title="Steric hindrance">steric hindrance</a> if it could not occupy the hole (such as <a href="/wiki/2,3-Bisphosphoglycerate" class="mw-redirect" title="2,3-Bisphosphoglycerate">BPG</a> in <a href="/wiki/Hemoglobin" title="Hemoglobin">hemoglobin</a>). Enzymes that catalyse multi-step reactions can have multiple oxyanion holes that stabilise different transition states in the reaction.<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> </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=Oxyanion_hole&amp;action=edit&amp;section=1" 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/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Transition_state" title="Transition state">Transition state</a></li> <li><a href="/wiki/Serine_proteases#Catalytic_mechanism" class="mw-redirect" title="Serine proteases">Serine proteases#Catalytic mechanism</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=Oxyanion_hole&amp;action=edit&amp;section=2" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap"><ol class="references"> <li id="cite_note-Stryer_Ch9-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-Stryer_Ch9_1-0">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFStryerBergTymoczko2002" class="citation book cs1">Stryer L, Berg JM, Tymoczko JL (2002). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK22526/">"9 Catalytic Strategies"</a>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/NBK21154/"><i>Biochemistry</i></a> (5th&#160;ed.). San Francisco: W.H. Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a>&#160;<a href="/wiki/Special:BookSources/978-0-7167-4955-4" title="Special:BookSources/978-0-7167-4955-4"><bdi>978-0-7167-4955-4</bdi></a>.</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=9+Catalytic+Strategies&amp;rft.btitle=Biochemistry&amp;rft.place=San+Francisco&amp;rft.edition=5th&amp;rft.pub=W.H.+Freeman&amp;rft.date=2002&amp;rft.isbn=978-0-7167-4955-4&amp;rft.aulast=Stryer&amp;rft.aufirst=L&amp;rft.au=Berg%2C+JM&amp;rft.au=Tymoczko%2C+JL&amp;rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fbooks%2FNBK22526%2F&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AOxyanion+hole" 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 id="CITEREFSimónGoodman2010" class="citation journal cs1">Simón, Luis; Goodman, Jonathan M. (March 19, 2010). "Enzyme Catalysis by Hydrogen Bonds: The Balance between Transition State Binding and Substrate Binding in Oxyanion Holes". <i>The Journal of Organic Chemistry</i>. <b>75</b> (6): 1831–1840. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fjo901503d">10.1021/jo901503d</a>. <a href="/wiki/ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a>&#160;<a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/0022-3263">0022-3263</a>. <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/20039621">20039621</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=The+Journal+of+Organic+Chemistry&amp;rft.atitle=Enzyme+Catalysis+by+Hydrogen+Bonds%3A+The+Balance+between+Transition+State+Binding+and+Substrate+Binding+in+Oxyanion+Holes&amp;rft.volume=75&amp;rft.issue=6&amp;rft.pages=1831-1840&amp;rft.date=2010-03-19&amp;rft.issn=0022-3263&amp;rft_id=info%3Apmid%2F20039621&amp;rft_id=info%3Adoi%2F10.1021%2Fjo901503d&amp;rft.aulast=Sim%C3%B3n&amp;rft.aufirst=Luis&amp;rft.au=Goodman%2C+Jonathan+M.&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AOxyanion+hole" 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 id="CITEREFMénardStorer1992" class="citation journal cs1">Ménard, Robert; Storer, Andrew C. (1992). "Oxyanion Hole Interactions in Serine and Cysteine Proteases". <i>Biological Chemistry Hoppe-Seyler</i>. <b>373</b> (2): 393–400. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1515%2Fbchm3.1992.373.2.393">10.1515/bchm3.1992.373.2.393</a>. <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/1387535">1387535</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=Biological+Chemistry+Hoppe-Seyler&amp;rft.atitle=Oxyanion+Hole+Interactions+in+Serine+and+Cysteine+Proteases&amp;rft.volume=373&amp;rft.issue=2&amp;rft.pages=393-400&amp;rft.date=1992&amp;rft_id=info%3Adoi%2F10.1515%2Fbchm3.1992.373.2.393&amp;rft_id=info%3Apmid%2F1387535&amp;rft.aulast=M%C3%A9nard&amp;rft.aufirst=Robert&amp;rft.au=Storer%2C+Andrew+C.&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AOxyanion+hole" 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="CITEREFKursulaOjalaLambeirWierenga2002" class="citation journal cs1">Kursula, Petri; Ojala, Juha; Lambeir, Anne-Marie; Wierenga, Rik K. (December 1, 2002). "The Catalytic Cycle of Biosynthetic Thiolase: A Conformational Journey of an Acetyl Group through Four Binding Modes and Two Oxyanion Holes‡". <i>Biochemistry</i>. <b>41</b> (52): 15543–15556. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi0266232">10.1021/bi0266232</a>. <a href="/wiki/ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a>&#160;<a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/0006-2960">0006-2960</a>. <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/12501183">12501183</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=Biochemistry&amp;rft.atitle=The+Catalytic+Cycle+of+Biosynthetic+Thiolase%3A+A+Conformational+Journey+of+an+Acetyl+Group+through+Four+Binding+Modes+and+Two+Oxyanion+Holes%E2%80%A1&amp;rft.volume=41&amp;rft.issue=52&amp;rft.pages=15543-15556&amp;rft.date=2002-12-01&amp;rft.issn=0006-2960&amp;rft_id=info%3Apmid%2F12501183&amp;rft_id=info%3Adoi%2F10.1021%2Fbi0266232&amp;rft.aulast=Kursula&amp;rft.aufirst=Petri&amp;rft.au=Ojala%2C+Juha&amp;rft.au=Lambeir%2C+Anne-Marie&amp;rft.au=Wierenga%2C+Rik+K.&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AOxyanion+hole" class="Z3988"></span></span> </li> </ol></div></div> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAlbert_Lehninger2008" class="citation book cs1"><a href="/wiki/Albert_Lehninger" class="mw-redirect" title="Albert Lehninger">Albert Lehninger</a>; et&#160;al. (2008). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=5Ek9J4p3NfkC&amp;q=albert+lehninger"><i>Principles of Biochemistry</i></a> (5th&#160;ed.). Macmillan. p.&#160;207. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a>&#160;<a href="/wiki/Special:BookSources/9780716771081" title="Special:BookSources/9780716771081"><bdi>9780716771081</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=Principles+of+Biochemistry&amp;rft.pages=207&amp;rft.edition=5th&amp;rft.pub=Macmillan&amp;rft.date=2008&amp;rft.isbn=9780716771081&amp;rft.au=Albert+Lehninger&amp;rft_id=https%3A%2F%2Fbooks.google.com%2Fbooks%3Fid%3D5Ek9J4p3NfkC%26q%3Dalbert%2Blehninger&amp;rfr_id=info%3Asid%2Fen.wikipedia.org%3AOxyanion+hole" class="Z3988"></span></li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist 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href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzymes" title="Template talk:Enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzymes" title="Special:EditPage/Template:Enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzymes" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a class="mw-selflink selflink">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li><b>EC7 <a 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> <!-- NewPP limit report Parsed by mw‐web.codfw.main‐f69cdc8f6‐d7pw2 Cached time: 20241122150111 Cache expiry: 2592000 Reduced expiry: false Complications: [vary‐revision‐sha1] 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