Escherichia coli K-12 substr. MG1655 Enzyme: trans-2-enoyl-CoA reductase

Subunit composition of trans-2-enoyl-CoA reductase = [subunit of trans-2-enoyl-CoA reductase (NADPH)]2

There is no gene yet identified for this enzyme.

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Enzymatic reaction of: trans-2-enoyl-CoA reductase

Synonyms: acyl-CoA:NADP+ trans-2-oxidoreductase

EC Number:

a 2,3,4-saturated fatty acyl CoA + NADP+ <=> a trans-2-enoyl-CoA + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is irreversible in the direction shown.

Alternative Substrates [Comment 1]:

NADPH-dependent trans-2-enoyl-CoA reductase is distinct from the three other enoyl-CoA reductases in E. coli. The reductase may participate in the chain elongation or degradation of fatty acids. This reaction is similar to the acyl-CoA dehydrogenase reaction, the fadE gene product. There is no gene associated with this enzyme as yet. [Mizugaki82, Nishimaki84]

Inhibitors (Competitive): NADP+ [Nishimaki84, Comment 2] , saturated acyl-CoA [Nishimaki84]

Inhibitors (Unknown Mechanism): p-hydroxymercuribenzoate [Nishimaki84] , N-ethylmaleimide [Nishimaki84] , 5,5'-dithio-bis-2-nitrobenzoate [Nishimaki84]


Mizugaki82: Mizugaki M, Nishimaki T, Shiraishi T, Kawaguchi A, Okuda S, Yamanaka H (1982). "Studies on the metabolism of unsaturated fatty acids. IX. Stereochemical studies of the reaction catalyzed by trans-2-enoyl-coenzyme A reductase of Escherichia coli." J Biochem (Tokyo) 1982;92(5);1649-54. PMID: 6759504

Nishimaki84: Nishimaki T, Yamanaka H, Mizugaki M (1984). "Studies on the metabolism of unsaturated fatty acids. XIV. Purification and properties of NADPH-dependent trans-2-enoyl-CoA reductase of Escherichia coli K-12." J Biochem (Tokyo) 1984;95(5);1315-21. PMID: 6378898

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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