Palmitoyl-CoA Hydrolase

"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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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.

Descriptor ID

D010170

MeSH Number(s)

D08.811.277.352.897.700

Concept/Terms

Palmitoyl-CoA Hydrolase

Acyl CoA Hydrolase

Thioesterase I

Below are MeSH descriptors whose meaning is more general than "Palmitoyl-CoA Hydrolase".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Hydrolases [D08.811.277]
Esterases [D08.811.277.352]
Thiolester Hydrolases [D08.811.277.352.897]
Palmitoyl-CoA Hydrolase [D08.811.277.352.897.700]

Below are MeSH descriptors whose meaning is related to "Palmitoyl-CoA Hydrolase".

Below are MeSH descriptors whose meaning is more specific than "Palmitoyl-CoA Hydrolase".

publications

Timeline | Most Recent

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.

Below are the most recent publications written about "Palmitoyl-CoA Hydrolase" by people in Profiles.

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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Probing enzyme promiscuity of SGNH hydrolases. Chembiochem. 2010 Oct 18; 11(15):2158-67.

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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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