Enoyl-CoA hydratase
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='1mj3' size=' | + | <StructureSection load='1mj3' size='350' side='right' caption='Structure of enoyl-CoA hydratase complex with hexadienoyl-CoA (PDB code [[1mj3]]).' scene='59/594523/Cv/1'> |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | ECH active site binds the substrate analog hexadienoyl-CoA<ref>PMID:12445775</ref>. | + | <scene name='59/594523/Cv/2'>Rat ECH is homohexamer</scene>; <scene name='59/594523/Cv/3'>another view for homohexamer</scene>. ECH active site binds the substrate analog hexadienoyl-CoA<ref>PMID:12445775</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 14:24, 21 January 2016
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3D structures of enoyl-CoA hydratase
Updated on 21-January-2016
References
- ↑ Agnihotri G, Liu HW. Enoyl-CoA hydratase. reaction, mechanism, and inhibition. Bioorg Med Chem. 2003 Jan 2;11(1):9-20. PMID:12467702
- ↑ 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
