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Thioesterase
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<h2 id="family">Family</h2> <p>The thioesterase activity is performed by members of the <a href="/facts/Acyl-CoA/uWNxxzSj">acyl-CoA</a> thioesterase (ACOT) family. The regulatory role of ACOT in <a href="/facts/Fatty_acid_metabolism/Se3rnCT8">fatty acid metabolism</a> depends on their <a href="/facts/Substrate_(biology)/EBDd458H">substrate</a> specificity, tissue expression and subcellular localization. For example, deactivation of <a href="/facts/Fatty_acid/JGg3erIu">fatty acids</a> at the ER may traffic fatty acids away from pathways associated with the ER membrane, such as <a href="/facts/Glycerolipid/TdQR87HX">glycerolipid</a> <a href="/facts/Biosynthesis/aFk7Tk7f">biosynthesis</a>. Two structurally different ACOT types lead to a similar <a href="/facts/Enzymatic/DSI1Fh7y">enzymatic</a> activity <a href="/facts/In_vitro/evp3hAX6">in vitro</a>, dividing the family into type I and type II ACOTs.<a class="footnote-ref" id="fnref:1" href="#fn:1"><sup>1</sup></a> </p><p>Type I ACOTs (ACOT1–6) contain the α/β-hydrolase domain, which is also present in many lipases and esterases . </p><p>Type II ACOTs (ACOT7–15) have a characteristic structural motif called the ‘<a href="/facts/HotDog_domain/XKJDwFD8">Hotdog fold</a>’ domain . </p> <h2 id="examples">Examples</h2> <p><a href="/facts/Acetyl-CoA_hydrolase/C0t7UU3A">Acetyl-CoA hydrolase</a>, <a href="/facts/Palmitoyl_protein_thioesterase/fy8mNoMC">palmitoyl-CoA hydrolase</a>, <a href="/facts/Succinyl-CoA_hydrolase/f3UtAwtC">succinyl-CoA hydrolase</a>, <a href="/facts/Formyl-CoA_hydrolase/4BPGqeNI">formyl-CoA hydrolase</a>, <a href="/facts/Acyl-CoA_hydrolase/WDxgV96d">acyl-CoA hydrolase</a> are a few examples of this group of enzymes. </p><p><a href="/facts/Ubiquitin_thiolesterase/6IFI89lX">Ubiquitin thiolesterase</a> is a well-known example, whose structure has been analyzed. </p><p>Humans genes which encode thioesterases include:<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a> </p><p><a href="/facts/ACOT1/TNUHJr19">ACOT1</a>, <a href="/facts/ACOT2/P5gGmYwf">ACOT2</a>, <a href="/facts/ACOT4/FrQj4yVp">ACOT4</a>, <a href="/facts/ACOT6/6PKltrgh">ACOT6</a>, <a href="/facts/ACOT7/SEAbPyvP">ACOT7</a>, <a href="/facts/ACOT8/JIp2eaV5">ACOT8</a>, <a href="/facts/ACOT9/oy5UxmqR">ACOT9</a>, <a href="/facts/ACOT11/Xp7mfTqc">ACOT11</a> (STARD14), <a href="/facts/ACOT12/K6hTmC4y">ACOT12</a> (STARD15), OLAH, <a href="/facts/PPT1/RC6N73wW">PPT1</a>, <a href="/facts/PPT2/19erKl2R">PPT2</a>, <a href="/facts/THEM2/BS4A9nw0">THEM2</a> (ACOT13), THEM4, THEM4P1, THEM5 </p> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=thioesterase+I">thioesterase+I</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li> <li><a href="https://meshb.nlm.nih.gov/record/ui?name=thioesterase+II">thioesterase+II</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Steensels S, Ersoy B. Fatty acid activation in thermogenic adipose tissue. Biochim Biophys Acta, 2018 May 21. <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Brocker, C; Carpenter, C; Nebert, DW; Vasiliou, V (Aug 2010). "Evolutionary divergence and functions of the human acyl-CoA thioesterase gene ( ACOT ) family". Human Genomics. 4 (6): 411–20. doi:10.1186/1479-7364-4-6-411. PMC 3525216. PMID 20846931. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525216" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3525216</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> </ol>