Enoyl-CoA hydratase

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== Structural highlights ==
== Structural highlights ==
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<scene name='59/594523/Cv/2'>Rat ECH is homohexamer</scene>; <scene name='59/594523/Cv/3'>another view for homohexamer</scene>. ECH <scene name='59/594523/Cv/6'>active site binds the substrate analog hexadienoyl-CoA</scene>. <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 <scene name='59/594523/Cv/7'>active site binds the substrate analog hexadienoyl-CoA</scene>. <ref>PMID:12445775</ref>
</StructureSection>
</StructureSection>

Revision as of 09:33, 11 March 2019

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

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3D structures of enoyl-CoA hydratase

Updated on 11-March-2019


References

  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. ↑ 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
  3. ↑ 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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Michal Harel, Alexander Berchansky

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