"Palmitoyl-CoA Hydrolase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.
Concept/Terms
Palmitoyl-CoA Hydrolase- Palmitoyl-CoA Hydrolase
- Hydrolase, Palmitoyl-CoA
- Palmitoyl CoA Hydrolase
- Oleoyl-CoA Acylhydrolase
- Acylhydrolase, Oleoyl-CoA
- Oleoyl CoA Acylhydrolase
- Palmitoyl CoA Deacylase
- CoA Deacylase, Palmitoyl
- Deacylase, Palmitoyl CoA
- Long-Chain Fatty-Acyl-CoA Hydrolase
- Fatty-Acyl-CoA Hydrolase, Long-Chain
- Hydrolase, Long-Chain Fatty-Acyl-CoA
- Long Chain Fatty Acyl CoA Hydrolase
- Palmitoyl Coenzyme A Hydrolase
- Palmitoyl Thioesterase
- Thioesterase, Palmitoyl
- Stearoyl CoA Hydrolase
- CoA Hydrolase, Stearoyl
- Hydrolase, Stearoyl CoA
- Fatty Acyl Thioesterase
- Thioesterase, Fatty Acyl
Below are MeSH descriptors whose meaning is more general than "Palmitoyl-CoA Hydrolase".
Below are MeSH descriptors whose meaning is more specific than "Palmitoyl-CoA Hydrolase".
This graph shows the total number of publications written about "Palmitoyl-CoA Hydrolase" by people in Harvard Catalyst Profiles by year, and whether "Palmitoyl-CoA Hydrolase" was a major or minor topic of these publication.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 1 | 0 | 1 |
| 2000 | 0 | 1 | 1 |
| 2001 | 1 | 0 | 1 |
| 2006 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2011 | 1 | 0 | 1 |
| 2012 | 2 | 0 | 2 |
| 2017 | 1 | 0 | 1 |
| 2020 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
Below are the most recent publications written about "Palmitoyl-CoA Hydrolase" by people in Profiles.
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Thioesterase superfamily member 1 undergoes stimulus-coupled conformational reorganization to regulate metabolism in mice. Nat Commun. 2021 06 09; 12(1):3493.
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Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine. Proc Natl Acad Sci U S A. 2020 09 08; 117(36):22080-22089.
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Regulation of fatty acid trafficking in liver by thioesterase superfamily member 1. J Lipid Res. 2018 02; 59(2):368-379.
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Functional characterization of thioesterase superfamily member 1/Acyl-CoA thioesterase 11: implications for metabolic regulation. J Lipid Res. 2012 Dec; 53(12):2620-31.
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Targeted deletion of thioesterase superfamily member 1 promotes energy expenditure and protects against obesity and insulin resistance. Proc Natl Acad Sci U S A. 2012 Apr 03; 109(14):5417-22.
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Inhibiting the palmitoylation/depalmitoylation cycle selectively reduces the growth of hematopoietic cells expressing oncogenic Nras. Blood. 2012 Jan 26; 119(4):1032-5.
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Terminal alkene formation by the thioesterase of curacin A biosynthesis: structure of a decarboxylating thioesterase. J Biol Chem. 2011 Apr 22; 286(16):14445-54.
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The endogenous inhibitor of Akt, CTMP, is critical to ischemia-induced neuronal death. Nat Neurosci. 2009 May; 12(5):618-26.
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The acyl-CoA thioesterase I is regulated by PPARalpha and HNF4alpha via a distal response element in the promoter. J Lipid Res. 2007 Aug; 48(8):1781-91.
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SNAP-23 and syntaxin-2 localize to the extracellular surface of the platelet plasma membrane. Blood. 2007 Sep 01; 110(5):1492-501.