Enoyl-CoA hydratase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Enoyl-CoA hydratase''' (ECH) is part of the fatty acid metabolism ([[Beta oxidation]]). ECH hydrates the double bond between the second and third carbons in acyl-CoA. ECH1 or short-chain ECH is mitochondrial. ECH1 processes enoyl-CoA thioesters from C4 to C16<ref>PMID:12467702</ref>. '''Enoyl-CoA hydratase/isomerase''' catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA in the last step of the methanethiol pathway of dimethyl-sulphoniopropionate catabolism<ref>PMID:23704947</ref>. | + | '''Enoyl-CoA hydratase''' (ECH) (gene '''rpfF''') is part of the fatty acid metabolism ([[Beta oxidation]]). ECH hydrates the double bond between the second and third carbons in acyl-CoA. ECH1 or short-chain ECH is mitochondrial. ECH1 processes enoyl-CoA thioesters from C4 to C16<ref>PMID:12467702</ref>. '''Enoyl-CoA hydratase/isomerase''' catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA in the last step of the methanethiol pathway of dimethyl-sulphoniopropionate catabolism<ref>PMID:23704947</ref>. |
== Disease == | == Disease == | ||
Revision as of 09:51, 21 February 2023
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References
- ↑ Agnihotri G, Liu HW. Enoyl-CoA hydratase. reaction, mechanism, and inhibition. Bioorg Med Chem. 2003 Jan 2;11(1):9-20. PMID:12467702
- ↑ Tan D, Crabb WM, Whitman WB, Tong L. Crystal Structure of DmdD, a Crotonase Superfamily Enzyme That Catalyzes the Hydration and Hydrolysis of Methylthioacryloyl-CoA. PLoS One. 2013 May 21;8(5):e63870. doi: 10.1371/journal.pone.0063870. Print 2013. PMID:23704947 doi:10.1371/journal.pone.0063870
- ↑ Sakai C, Yamaguchi S, Sasaki M, Miyamoto Y, Matsushima Y, Goto Y. ECHS1 mutations cause combined respiratory chain deficiency resulting in Leigh syndrome. Hum Mutat. 2015 Feb;36(2):232-9. doi: 10.1002/humu.22730. PMID:25393721 doi:http://dx.doi.org/10.1002/humu.22730
- ↑ Bell AF, Feng Y, Hofstein HA, Parikh S, Wu J, Rudolph MJ, Kisker C, Whitty A, Tonge PJ. Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers. Chem Biol. 2002 Nov;9(11):1247-55. PMID:12445775
