Enoyl-CoA hydratase

Function

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. It processes enoyl-CoA thioesters from C4 to C16^[1].
ECH2 hydrates enoyl-CoA to 3-hydroxyacyl-CoA in the oxidation of fatty acids pathway^[2].
Enoyl-CoA hydratase/isomerase catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA in the last step of the methanethiol pathway of dimethyl-sulphoniopropionate catabolism^[3].

Disease

ECH1 mutations cause combined respiratory chain deficiency resulting inn Leigh syndrome^[4].

Structural highlights

; . ECH . ^[5]

3D structures of enoyl-CoA hydratase

Enoyl-CoA hydratase 3D structures

Structure of enoyl-CoA hydratase complex with hexadienoyl-CoA (PDB code 1mj3).

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Agnihotri G, Liu HW. Enoyl-CoA hydratase. reaction, mechanism, and inhibition. Bioorg Med Chem. 2003 Jan 2;11(1):9-20. PMID:12467702
↑ Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T. A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2. J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:15051722 doi:10.1074/jbc.M400293200
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] Agnihotri G, Liu HW. Enoyl-CoA hydratase. reaction, mechanism, and inhibition. Bioorg Med Chem. 2003 Jan 2;11(1):9-20. PMID:12467702

[2] Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T. A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2. J Biol Chem. 2004 Jun 4;279(23):24666-72. Epub 2004 Mar 29. PMID:15051722 doi:10.1074/jbc.M400293200

[3] 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

[4] 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

[5] 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

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Enoyl-CoA hydratase

Contents

Function

Disease

Structural highlights

3D structures of enoyl-CoA hydratase

ReferencesReferences

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Enoyl-CoA hydratase

Function

Disease

Structural highlights

3D structures of enoyl-CoA hydratase

ReferencesReferences

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