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<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 class="cdx-message cdx-message--block cdx-message--warning mw-revision"><span class="cdx-message__icon"></span><div class="cdx-message__content"><div id="mw-revision-info-current"><p><b>This is the <a href="/wiki/Help:Page_history" title="Help:Page history">current revision</a> of this page, as edited by <span id="mw-revision-name"><a href="/wiki/User:Citation_bot" class="mw-userlink" title="User:Citation bot" data-mw-revid="1188199430"><bdi>Citation bot</bdi></a> <span class="mw-usertoollinks">(<a href="/wiki/User_talk:Citation_bot" class="mw-usertoollinks-talk" title="User talk:Citation bot">talk</a> | <a href="/wiki/Special:Contributions/Citation_bot" class="mw-usertoollinks-contribs" title="Special:Contributions/Citation bot">contribs</a>)</span></span> at <span id="mw-revision-date">22:52, 3 December 2023</span><span id="mw-revision-summary"> <span class="comment">(Add: doi-access. | <a href="/wiki/Wikipedia:UCB" class="mw-redirect" title="Wikipedia:UCB">Use this bot</a>. <a href="/wiki/Wikipedia:DBUG" class="mw-redirect" title="Wikipedia:DBUG">Report bugs</a>. | #UCB_CommandLine)</span></span>. The present address (URL) is a <a href="/wiki/Help:Permanent_link" title="Help:Permanent link">permanent link</a> to this version.</b></p><div id="revision-info-current-plain" style="display: none;">Revision as of 22:52, 3 December 2023 by <a href="/wiki/User:Citation_bot" class="mw-userlink" title="User:Citation bot" data-mw-revid="1188199430"><bdi>Citation bot</bdi></a> <span class="mw-usertoollinks">(<a href="/wiki/User_talk:Citation_bot" class="mw-usertoollinks-talk" title="User talk:Citation bot">talk</a> | <a href="/wiki/Special:Contributions/Citation_bot" class="mw-usertoollinks-contribs" title="Special:Contributions/Citation bot">contribs</a>)</span> <span class="comment">(Add: doi-access. | <a href="/wiki/Wikipedia:UCB" class="mw-redirect" title="Wikipedia:UCB">Use this bot</a>. <a href="/wiki/Wikipedia:DBUG" class="mw-redirect" title="Wikipedia:DBUG">Report bugs</a>. | #UCB_CommandLine)</span></div></div><div id="mw-revision-nav">(<a href="/w/index.php?title=Demethylase&diff=prev&oldid=1188199430" title="Demethylase">diff</a>) <a href="/w/index.php?title=Demethylase&direction=prev&oldid=1188199430" title="Demethylase">← Previous revision</a> | Latest revision (diff) | Newer revision → (diff)</div></div></div></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">Enzymes that remove methyl (CH3-) groups from nucleic acids</div> <p><b>Demethylases</b> are <a href="/wiki/Enzymes" class="mw-redirect" title="Enzymes">enzymes</a> that remove <a href="/wiki/Methyl" class="mw-redirect" title="Methyl">methyl</a> (CH<sub>3</sub>) groups from <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acids</a>, proteins (particularly <a href="/wiki/Histone" title="Histone">histones</a>), and other molecules. Demethylases are important <a href="/wiki/Epigenetics" title="Epigenetics">epigenetic</a> proteins, as they are responsible for <a href="/wiki/Transcriptional_regulation" title="Transcriptional regulation">transcriptional regulation</a> of the <a href="/wiki/Genome" title="Genome">genome</a> by controlling the <a href="/wiki/Methylation" title="Methylation">methylation</a> of DNA and histones, and by extension, the <a href="/wiki/Chromatin" title="Chromatin">chromatin</a> state at specific <a href="/wiki/Gene" title="Gene">gene</a> loci. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Histone_lysine_demethylation">Histone lysine demethylation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Demethylase&action=edit&section=1" title="Edit section: Histone lysine demethylation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Lysine_demethylation.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/d/d4/Lysine_demethylation.svg/400px-Lysine_demethylation.svg.png" decoding="async" width="400" height="406" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/d/d4/Lysine_demethylation.svg/600px-Lysine_demethylation.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/d/d4/Lysine_demethylation.svg/800px-Lysine_demethylation.svg.png 2x" data-file-width="512" data-file-height="520" /></a><figcaption>Lysine demethylatiuon mechanisms of histone lysine demethylase 1A (KDM1A) and the JmjC-domain-containing histone lysine demethylases (JHDMs). Both mechanisms involve the oxidation of a methyl group (with <a href="/wiki/FAD" class="mw-redirect" title="FAD">FAD</a> or <a href="/wiki/%CE%91-ketoglutarate" class="mw-redirect" title="Α-ketoglutarate">α-ketoglutarate</a> as cofactors) followed by the elimination of <a href="/wiki/Formaldehyde" title="Formaldehyde">formaldehyde</a>. The mechanism of KDM1A and KDM1B is dependent on the formation of an iminium intermediate and therefore they may only demethylate mono- and dimethylated lysine substrates. </figcaption></figure> <p><a href="/wiki/Histone_methylation" title="Histone methylation">Histone methylation</a> was initially considered an effectively irreversible process as the half-life of the histone methylation was approximately equal to the histone half-life.<sup id="cite_ref-Ped_1-0" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Histone lysine demethylase LSD1 (later classified as KDM1A) was first identified in 2004 as a nuclear amine oxidase homolog.<sup id="cite_ref-shi_2-0" class="reference"><a href="#cite_note-shi-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Two main classes of histone lysine demethylases exist, defined by their mechanisms: <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">flavin adenine dinucleotide (FAD)</a>-dependent <a href="/wiki/Amine_oxidase" title="Amine oxidase">amine oxidases</a> and <a href="/wiki/Alpha-ketoglutarate-dependent_hydroxylase" class="mw-redirect" title="Alpha-ketoglutarate-dependent hydroxylase">α-ketoglutarate-dependent hydroxylases</a>. </p><p>Histone lysine demethylases possess a variety of <a href="/wiki/Protein_domain" title="Protein domain">domains</a> that are responsible for histone recognition, DNA binding, methylated <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> substrate binding and catalytic activity. These include: </p> <ul><li>FAD-dependent amine oxidase domains containing the active catalytic site of KDM1</li> <li>Jumonji-C domains containing the active catalytic site of KDM2 through KDM8<sup id="cite_ref-MOS_3-0" class="reference"><a href="#cite_note-MOS-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-aprelikova_4-0" class="reference"><a href="#cite_note-aprelikova-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup></li> <li>Jumonji-N domains responsible for Jumonji-C domain conformation stability</li> <li>SWIRM (SWI3P, RSC8P and Moira) domains proposed as an anchor site for histone substrates and responsible for <a href="/wiki/Chromatin" title="Chromatin">chromatin</a> stability</li> <li>PHD, CXXC and C5HC2 <a href="/wiki/Zinc_finger" title="Zinc finger">zinc finger</a> domains responsible for histone recognition and binding</li></ul><p> Histone lysine demethylases are classified according to their domains and unique substrate specificities. The lysine substrates and identified according to their position in the corresponding histone amino acid sequence and methylation state (for example, H3K9me3 refers to trimethylated histone 3 lysine 9.) </p><figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Jmjd2a(2UXX)_with_domains_highlighted.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/be/Jmjd2a%282UXX%29_with_domains_highlighted.png/220px-Jmjd2a%282UXX%29_with_domains_highlighted.png" decoding="async" width="220" height="262" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/b/be/Jmjd2a%282UXX%29_with_domains_highlighted.png/330px-Jmjd2a%282UXX%29_with_domains_highlighted.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/b/be/Jmjd2a%282UXX%29_with_domains_highlighted.png/440px-Jmjd2a%282UXX%29_with_domains_highlighted.png 2x" data-file-width="3550" data-file-height="4220" /></a><figcaption>Structure of JmJDA (coordinates from PDB file:2UXX); Some domains from above are highlighted: JmJ(N-terminus, red; C-terminus, yellow), Zinc finger domain (light purple), Beta-hairpin (light blue), and mixed domain linker (green).</figcaption></figure> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Lysine_specific_demethylase_1.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/0/0b/Lysine_specific_demethylase_1.png/220px-Lysine_specific_demethylase_1.png" decoding="async" width="220" height="198" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/0b/Lysine_specific_demethylase_1.png/330px-Lysine_specific_demethylase_1.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/0b/Lysine_specific_demethylase_1.png/440px-Lysine_specific_demethylase_1.png 2x" data-file-width="890" data-file-height="800" /></a><figcaption>Structure of KDM1A (coordinates from PDB file:2Z5U)</figcaption></figure> <dl><dt><b>KDM1</b></dt> <dd>The KDM1 homologs include <a href="/wiki/KDM1A" title="KDM1A">KDM1A</a> and <a href="/wiki/KDM1B" title="KDM1B">KDM1B</a>. KDM1A demethylates H3K4me1/2 and H3K9me1/2, and KDM1B emethylates H3K4me1/2. KDM1 activity is critical to <a href="/wiki/Embryogenesis" class="mw-redirect" title="Embryogenesis">embryogenesis</a> and tissue-specific <a href="/wiki/Cellular_differentiation" title="Cellular differentiation">differentiation</a>, as well as oocyte growth.<sup id="cite_ref-Ped_1-1" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Deletion of the gene for KDM1A can have effects on the growth and differentiation of <a href="/wiki/Embryonic_stem_cells" class="mw-redirect" title="Embryonic stem cells">embryonic stem cells</a> and is universally lethal in <a href="/wiki/Knockout_mouse" title="Knockout mouse">knockout mice</a>.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> KDM1A gene expression is observed to be upregulated in some cancers,<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> and so KDM1A inhibition has therefore been considered a possible epigenetic treatment for cancer.<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup>:KDM1B, however, is mostly involved in <a href="/wiki/Oocyte" title="Oocyte">oocyte</a> development. Deletion of this gene leads to <a href="/wiki/Maternal_effect" title="Maternal effect">maternal effect</a> lethality in mice.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> Orthologs of KDM1 in <i><a href="/wiki/Drosophila_melanogaster" title="Drosophila melanogaster">D. melanogaster</a></i> and <i><a href="/wiki/Caenorhabditis_elegans" title="Caenorhabditis elegans">C. elegans</a></i> appear to function similarly to KDM1B rather than KDM1A.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup></dd></dl> <dl><dt><b>KDM2</b></dt> <dd>The KDM2 homologs include <a href="/wiki/KDM2A" title="KDM2A">KDM2A</a> and <a href="/wiki/KDM2B" title="KDM2B">KDM2B</a>. KDM2A and KDM2B demethylate H3K4me3 and H3K36me2/3. KDM2A has roles in either promoting or inhibiting tumor function, and KDM2B has roles in <a href="/wiki/Oncogenesis" class="mw-redirect" title="Oncogenesis">oncogenesis</a>.<sup id="cite_ref-Ped_1-2" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> KDM2A and KDM2B possess CXXC zinc finger domains responsible for binding to unmethylated CpG islands, and it is believed that they may bind to many gene regulatory elements in the absence of sequence-specific transcription factors.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup>:Overexpressed KDM2B has been observed in human <a href="/wiki/Lymphomas" class="mw-redirect" title="Lymphomas">lymphoma</a> and <a href="/wiki/Adenocarcinomas" class="mw-redirect" title="Adenocarcinomas">adenocarcinoma</a>, and underexpressed KDM2B has been observed in human prostate cancer and glioblastoma. KDM2B has been additionally shown to prevent <a href="/wiki/Senescence" title="Senescence">senescence</a> in some cells through <a href="/wiki/Ectopic_expression" title="Ectopic expression">ectopic expression</a>.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup></dd></dl> <dl><dt><b>KDM3</b></dt> <dd>The KDM3 homologs include <a href="/wiki/KDM3A" title="KDM3A">KDM3A</a>, <a href="/wiki/KDM3B" title="KDM3B">KDM3B</a> and <a href="/wiki/JMJD1C" title="JMJD1C">KDM3C</a>. KDM3A, KDM3B and KDM3C demethylate H3K9me1/2. KDM3A has roles in <a href="/wiki/Spermatogenesis" title="Spermatogenesis">spermatogenesis</a> and metabolic functions, however, the activity of KDM3B and KDM3C are not specifically known.<sup id="cite_ref-Ped_1-3" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>:Knockdown studies of KDM3A in mice resulted in male infertility and adult onset-obesity. Additional studies have indicated that KDM3A may play a role in regulation of androgen receptor-dependent genes as well as genes involved in <a href="/wiki/Pluripotent" class="mw-redirect" title="Pluripotent">pluripotency</a>, indicating a potential role for KDM3A in tumorigenesis.<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup></dd></dl> <dl><dt><b>KDM4</b></dt> <dd>The KDM4 homologs include <a href="/wiki/KDM4A" title="KDM4A">KDM4A</a>, <a href="/wiki/KDM4B" title="KDM4B">KDM4B</a>, <a href="/wiki/KDM4C" title="KDM4C">KDM4C</a>, <a href="/wiki/KDM4D" title="KDM4D">KDM4D</a>, KDM4E and KDM4F. KDM4A, KDM4B and KDM4C demethylate H3K9me2/3, H3K9me3 and H3K36me2/3, and KDM4D, KDM4E and KDM4F demethylate H3K9me2/3. KDM4A, KDM4B, KDM4C and KDM4D have roles in <a href="/wiki/Tumorigenesis" class="mw-redirect" title="Tumorigenesis">tumorigenesis</a>, however, the activity of KDM4E and KDM4F are not specifically known..<sup id="cite_ref-Ped_1-4" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> KDM4B upregulation has bee observed in medulloblastoma, and KDM4C amplification has been documented in oesophageal squamous carcinoma, medulloblastoma and breast cancer.<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-21" class="reference"><a href="#cite_note-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Other gene expression data has also suggested KDM4A, KDM4B, and KDM4C are overexpressed in prostate cancer.<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup></dd></dl> <dl><dt><b>KDM5</b></dt> <dd>The KDM5 homologs includes <a href="/wiki/KDM5A" title="KDM5A">KDM5A</a>, <a href="/wiki/KDM5B" class="mw-redirect" title="KDM5B">KDM5B</a>, <a href="/wiki/KDM5C" title="KDM5C">KDM5C</a> and <a href="/wiki/KDM5D" title="KDM5D">KDM5D</a>. KDM5A, KDM5B, KDM5C and KDM5D demethylate H3K4me2/3.<sup id="cite_ref-Ped_1-5" class="reference"><a href="#cite_note-Ped-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> The KDM5 family appears to regulate key developmental functions, including cellular differentiation, <a href="/wiki/Mitochondria" class="mw-redirect" title="Mitochondria">mitochondrial</a> function and <a href="/wiki/Cell_cycle" title="Cell cycle">cell cycle</a> progression.<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-26" class="reference"><a href="#cite_note-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-27" class="reference"><a href="#cite_note-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-28" class="reference"><a href="#cite_note-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> KDM5B and KDM5C have also shown to interaction with PcG proteins, which are involved in transcriptional repression. KDM5C mutations on the X-chromosome have also been observed in patients with <a href="/wiki/X-linked" class="mw-redirect" title="X-linked">X-linked</a> intellectual disability.<sup id="cite_ref-29" class="reference"><a href="#cite_note-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> Depletion of KDM5C homologs in <i><a href="/wiki/D._rerio" class="mw-redirect" title="D. rerio">D. rerio</a></i> have shown brain-patterning defects and neuronal cell death.<sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup></dd></dl> <dl><dt><b>KDM6</b></dt> <dd>The KDM6 family includes <a href="/wiki/KDM6A" class="mw-redirect" title="KDM6A">KDM6A</a>, <a href="/wiki/KDM6B" title="KDM6B">KDM6B</a> and <a href="/wiki/UTY_(gene)" title="UTY (gene)">KDM6C</a>. KDM6A and KDM6B demethylate H3K27me2/3, and KDM4C demethylates H3K27me3. KDM6A and KDM6B possess tumor-suppressive characteristics. KDM6A knockdowns in <a href="/wiki/Fibroblast" title="Fibroblast">fibroblasts</a> lead to an immediate increase in fibroblast population. KDM6B expressed in fibroblasts induces oncogenes of the Ras/Raf/MEK/ERK pathway.<sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> Point mutations of KDM6A have been identified as one cause of <a href="/wiki/Kabuki_syndrome" title="Kabuki syndrome">Kabuki syndrome</a>, a congenital disorder resulting in intellectual disability.<sup id="cite_ref-32" class="reference"><a href="#cite_note-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> Deletion of KDM6A in <i><a href="/wiki/D._rerio" class="mw-redirect" title="D. rerio">D. rerio</a></i> results in decreased expression of HOX genes, which play a role in regulating <a href="/wiki/Regional_specification" class="mw-redirect" title="Regional specification">body patterning</a> during development.<sup id="cite_ref-34" class="reference"><a href="#cite_note-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> In mammalian studies, KDM6A has been shown to regulate HOX genes as well.<sup id="cite_ref-agg_35-0" class="reference"><a href="#cite_note-agg-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-36" class="reference"><a href="#cite_note-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> Mutation of KDM5B disrupt gonad development in <i>C.elegans</i>.<sup id="cite_ref-agg_35-1" class="reference"><a href="#cite_note-agg-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> Other studies have shown that KDM6B expression is upregulated in activated <a href="/wiki/Macrophages" class="mw-redirect" title="Macrophages">macrophages</a> and dynamically expressed during differentiation of <a href="/wiki/Stem_cells" class="mw-redirect" title="Stem cells">stem cells</a>.<sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-38" class="reference"><a href="#cite_note-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup></dd></dl> <div class="mw-heading mw-heading2"><h2 id="Ester_demethylation">Ester demethylation</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Demethylase&action=edit&section=2" title="Edit section: Ester demethylation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:1a2o_structure.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/6/69/1a2o_structure.png/220px-1a2o_structure.png" decoding="async" width="220" height="176" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/69/1a2o_structure.png/330px-1a2o_structure.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/69/1a2o_structure.png/440px-1a2o_structure.png 2x" data-file-width="2500" data-file-height="2000" /></a><figcaption>Cartoon representation of the molecular structure of protein registered with 1A2O pdb code.</figcaption></figure> <p>Another example of a demethylase is <a href="/wiki/Protein-glutamate_methylesterase" title="Protein-glutamate methylesterase">protein-glutamate methylesterase</a>, also known as CheB protein (EC 3.1.1.61), which demethylates MCPs (<b>m</b>ethyl-accepting <b>c</b>hemotaxis <b>p</b>roteins) through hydrolysis of carboxylic ester bonds. The association of a <a href="/wiki/Chemotaxis" title="Chemotaxis">chemotaxis</a> receptor with an agonist leads to the phosphorylation of CheB. Phosphorylation of CheB protein enhances its catalytic MCP demethylating activity resulting in adaption of the cell to environmental stimuli.<sup id="cite_ref-Vla_39-0" class="reference"><a href="#cite_note-Vla-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> MCPs respond to extracellular attractants and repellents in bacteria like <i><a href="/wiki/E._coli" class="mw-redirect" title="E. coli">E. coli</a></i> in <a href="/wiki/Chemotaxis" title="Chemotaxis">chemotaxis</a> regulation. CheB is more specifically termed a <a href="/wiki/Esterase" title="Esterase">methylesterase</a>, as it removes methyl groups from <a href="/wiki/Methylglutamate" class="mw-redirect" title="Methylglutamate">methylglutamate</a> residues located on the MCPs through hydrolysis, producing <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> accompanied by the release of <a href="/wiki/Methanol" title="Methanol">methanol</a>.<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup> </p><p>CheB is of particular interest to researchers as it may be a therapeutic target for mitigating the spread of bacterial infections.<sup id="cite_ref-41" class="reference"><a href="#cite_note-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-halign-none" typeof="mw:File/Frame"><a href="/wiki/File:Chemotaxis_Regulation_within_E._coli.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/3/32/Chemotaxis_Regulation_within_E._coli.png" decoding="async" width="550" height="217" class="mw-file-element" data-file-width="550" data-file-height="217" /></a><figcaption>Chemotaxis signalling. Chemoattractants or repellents are sensed by transmembrane receptors. Note the role of CheB (B) in demethylation of MCP receptors.<sup id="cite_ref-Vla_39-1" class="reference"><a href="#cite_note-Vla-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup></figcaption></figure> <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=Demethylase&action=edit&section=3" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Chemotaxis" title="Chemotaxis">Chemotaxis</a></li> <li><a href="/wiki/Esterase" title="Esterase">Esterase</a></li> <li><a href="/wiki/Transferase" title="Transferase">Transferase</a></li> <li><a href="/wiki/Methylase" class="mw-redirect" title="Methylase">Methylase</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=Demethylase&action=edit&section=4" 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: 33em;"> <ol class="references"> <li id="cite_note-Ped-1"><span class="mw-cite-backlink">^ <a href="#cite_ref-Ped_1-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Ped_1-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Ped_1-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Ped_1-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Ped_1-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Ped_1-5"><sup><i><b>f</b></i></sup></a></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="CITEREFPedersenHelin2010" class="citation journal cs1">Pedersen MT, Helin K (Nov 2010). 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"Reconstruction of the chemotaxis receptor-kinase assembly". <i>Nature Structural & Molecular Biology</i>. <b>13</b> (5): 400–7. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnsmb1085">10.1038/nsmb1085</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16622408">16622408</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:859928">859928</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Structural+%26+Molecular+Biology&rft.atitle=Reconstruction+of+the+chemotaxis+receptor-kinase+assembly&rft.volume=13&rft.issue=5&rft.pages=400-7&rft.date=2006-05&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A859928%23id-name%3DS2CID&rft_id=info%3Apmid%2F16622408&rft_id=info%3Adoi%2F10.1038%2Fnsmb1085&rft.aulast=Park&rft.aufirst=SY&rft.au=Borbat%2C+PP&rft.au=Gonzalez-Bonet%2C+G&rft.au=Bhatnagar%2C+J&rft.au=Pollard%2C+AM&rft.au=Freed%2C+JH&rft.au=Bilwes%2C+AM&rft.au=Crane%2C+BR&rfr_id=info%3Asid%2Fen.wikipedia.org%3ADemethylase" class="Z3988"></span></span> </li> <li id="cite_note-41"><span class="mw-cite-backlink"><b><a href="#cite_ref-41">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFWestMartinez-HackertStock1995" class="citation journal cs1">West AH, Martinez-Hackert E, Stock AM (Jul 1995). "Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB". <i>Journal of Molecular Biology</i>. <b>250</b> (2): 276–90. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1006%2Fjmbi.1995.0376">10.1006/jmbi.1995.0376</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7608974">7608974</a>.</cite><span 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href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.11_With_2-oxoglutarate_as_one_donor.2C_and_incorporation_of_one_atom_each_of_oxygen_into_both_donors" title="List of EC numbers (EC 1)">1.14.11</a>: <a href="/wiki/Alpha-Ketoglutaric_acid" class="mw-redirect" title="Alpha-Ketoglutaric acid">2-oxoglutarate</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Prolyl_hydroxylase" class="mw-redirect" title="Prolyl hydroxylase">Prolyl hydroxylase</a> <ul><li><a href="/wiki/HIF_prolyl-hydroxylase" class="mw-redirect" title="HIF prolyl-hydroxylase">HIF prolyl-hydroxylase</a> <ul><li><a href="/wiki/EGLN1" title="EGLN1">EGLN1</a></li> <li><a href="/wiki/EGLN2" title="EGLN2">EGLN2</a></li> <li><a href="/wiki/EGLN3" title="EGLN3">EGLN3</a></li></ul></li> <li><a href="/wiki/P4HTM" title="P4HTM">P4HTM</a></li></ul></li> <li><a href="/wiki/Lysyl_hydroxylase" title="Lysyl hydroxylase">Lysyl hydroxylase</a></li> <li><a href="/wiki/AlkB" title="AlkB">AlkB</a> <ul><li><a href="/wiki/Alkb_homolog_1,_histone_h2a_dioxygenase" title="Alkb homolog 1, histone h2a dioxygenase">ALKBH1</a></li> <li><a href="/wiki/FTO_gene" title="FTO gene">FTO</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.13_With_NADH_or_NADPH_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.13</a>: <a href="/wiki/NADH" class="mw-redirect" title="NADH">NADH</a> or <a href="/wiki/NADPH" class="mw-redirect" title="NADPH">NADPH</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Flavin-containing_monooxygenase" title="Flavin-containing monooxygenase">Flavin-containing monooxygenase</a> <ul><li><a href="/wiki/FMO1" class="mw-redirect" title="FMO1">FMO1</a></li> <li><a href="/wiki/FMO2" title="FMO2">FMO2</a></li> <li><a href="/wiki/Flavin-containing_monooxygenase_3" title="Flavin-containing monooxygenase 3">FMO3</a></li> <li><a href="/wiki/FMO4" title="FMO4">FMO4</a></li> <li><a href="/wiki/FMO5" title="FMO5">FMO5</a></li></ul></li> <li><a href="/wiki/Nitric_oxide_synthase" title="Nitric oxide synthase">Nitric oxide synthase</a> <ul><li><a href="/wiki/NOS1" title="NOS1">NOS1</a></li> <li><a href="/wiki/Nitric_oxide_synthase_2_(inducible)" title="Nitric oxide synthase 2 (inducible)">NOS2</a></li> <li><a href="/wiki/Endothelial_NOS" title="Endothelial NOS">NOS3</a></li></ul></li> <li><a href="/wiki/Cholesterol_7_alpha-hydroxylase" title="Cholesterol 7 alpha-hydroxylase">Cholesterol 7 alpha-hydroxylase</a></li> <li><a href="/wiki/Methane_monooxygenase" title="Methane monooxygenase">Methane monooxygenase</a></li> <li><a href="/wiki/CYP3A4" title="CYP3A4">3A4</a></li> <li><a href="/wiki/14%CE%B1-demethylase" class="mw-redirect" title="14α-demethylase">14α-demethylase</a></li> <li><a href="/wiki/24-hydroxycholesterol_7alpha-hydroxylase" title="24-hydroxycholesterol 7alpha-hydroxylase">24-hydroxycholesterol 7α-hydroxylase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.14_With_reduced_flavin_or_flavoprotein_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.14</a>: reduced <a href="/wiki/Flavin_group" title="Flavin group">flavin</a> or <a href="/wiki/Flavoprotein" title="Flavoprotein">flavoprotein</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Aromatase" title="Aromatase">19A1</a></li> <li><a href="/wiki/CYP2D6" title="CYP2D6">2D6</a></li> <li><a href="/wiki/CYP2E1" title="CYP2E1">2E1</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.15_With_reduced_iron–sulfur_protein_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.15</a>: reduced <a href="/wiki/Iron%E2%80%93sulfur_protein" title="Iron–sulfur protein">iron–sulfur protein</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Steroid_11-beta-hydroxylase" class="mw-redirect" title="Steroid 11-beta-hydroxylase">11B1</a></li> <li><a href="/wiki/Aldosterone_synthase" title="Aldosterone synthase">11B2</a></li> <li><a href="/wiki/Cholesterol_side-chain_cleavage_enzyme" title="Cholesterol side-chain cleavage enzyme">11A1</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.16_With_reduced_pteridine_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.16</a>: reduced <a href="/wiki/Pteridine" title="Pteridine">pteridine</a> (<a href="/wiki/Tetrahydrobiopterin" title="Tetrahydrobiopterin">BH4 dependent</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Phenylalanine_hydroxylase" title="Phenylalanine hydroxylase">Phenylalanine hydroxylase</a></li> <li><a href="/wiki/Tyrosine_hydroxylase" title="Tyrosine hydroxylase">Tyrosine hydroxylase</a></li> <li><a href="/wiki/Tryptophan_hydroxylase" title="Tryptophan hydroxylase">Tryptophan hydroxylase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.17_With_reduced_ascorbate_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.17</a>: reduced <a href="/wiki/Ascorbate" class="mw-redirect" title="Ascorbate">ascorbate</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Dopamine_beta-hydroxylase" title="Dopamine beta-hydroxylase">Dopamine beta-hydroxylase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.18_With_another_compound_as_one_donor.2C_and_incorporation_of_one_atom_of_oxygen" title="List of EC numbers (EC 1)">1.14.18</a>-<a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.19_With_oxidation_of_a_pair_of_donors_resulting_in_the_reduction_of_molecular_oxygen_to_two_molecules_of_water" title="List of EC numbers (EC 1)">19</a>: other</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/Tyrosinase" title="Tyrosinase">Tyrosinase</a></li> <li><a href="/wiki/Stearoyl-CoA_desaturase-1" class="mw-redirect" title="Stearoyl-CoA desaturase-1">Stearoyl-CoA desaturase-1</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_1)#EC_1.14.99_Miscellaneous" title="List of EC numbers (EC 1)">1.14.99</a> - miscellaneous</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/Cyclooxygenase" title="Cyclooxygenase">Cyclooxygenase</a></li> <li><a href="/wiki/Heme_oxygenase" title="Heme oxygenase">Heme oxygenase</a> (<a href="/wiki/HMOX1" title="HMOX1">HMOX1</a>)</li> <li><a href="/wiki/Squalene_monooxygenase" title="Squalene monooxygenase">Squalene monooxygenase</a></li> <li><a href="/wiki/CYP17A1" title="CYP17A1">17A1</a></li> <li><a href="/wiki/21-Hydroxylase" title="21-Hydroxylase">21A2</a></li> <li><a href="/wiki/Ecdysone_20-monooxygenase" title="Ecdysone 20-monooxygenase">Ecdysone 20-monooxygenase</a></li> <li><a href="/wiki/Deoxyhypusine_monooxygenase" title="Deoxyhypusine monooxygenase">Deoxyhypusine monooxygenase</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="Enzymes" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzymes" title="Template talk:Enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzymes" title="Special:EditPage/Template:Enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzymes" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li><b>EC7 <a 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> <style data-mw-deduplicate="TemplateStyles:r1130092004">.mw-parser-output .portal-bar{font-size:88%;font-weight:bold;display:flex;justify-content:center;align-items:baseline}.mw-parser-output .portal-bar-bordered{padding:0 2em;background-color:#fdfdfd;border:1px solid #a2a9b1;clear:both;margin:1em auto 0}.mw-parser-output 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