Structural highlights
Function
[ACOT2_HUMAN] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Acyl-CoA thioesterases (ACOTs) catalyze the hydrolysis of CoA esters to free CoA and carboxylic acids and have important functions in lipid metabolism and other cellular processes. Type I ACOTs are found only in animals and contain an alpha/beta hydrolase domain, through currently no structural information is available on any of these enzymes. We report here the crystal structure at 2.1A resolution of human mitochondrial ACOT2, a type I enzyme. The structure contains two domains, N and C domains. The C domain has the alpha/beta hydrolase fold, with the catalytic triad Ser294-His422-Asp388. The N domain contains a seven-stranded beta-sandwich, which has some distant structural homologs in other proteins. The active site is located in a large pocket at the interface between the two domains. The structural information has significant relevance for other type I ACOTs and related enzymes.
Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2).,Mandel CR, Tweel B, Tong L Biochem Biophys Res Commun. 2009 Aug 7;385(4):630-3. Epub 2009 Jun 2. PMID:19497300[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jones JM, Gould SJ. Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. PMID:10944470 doi:http://dx.doi.org/10.1006/bbrc.2000.3285
- ↑ Mandel CR, Tweel B, Tong L. Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2). Biochem Biophys Res Commun. 2009 Aug 7;385(4):630-3. Epub 2009 Jun 2. PMID:19497300 doi:10.1016/j.bbrc.2009.05.122