2-methyl-branched-chain-enoyl-CoA reductase

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In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.1.52) is an enzyme that catalyzes the chemical reaction

2-methylbutanoyl-CoA + NAD⁺ $\rightleftharpoons$ 2-methylcrotonoyl-CoA + NADH + H⁺

Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and NAD⁺, whereas its 3 products are 2-methylcrotonoyl-CoA, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-methyl-branched-chain-acyl-CoA:NAD+ 2-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. It employs one cofactor, FAD.

[edit] References

IUBMB entry for 1.3.1.52
BRENDA references for 1.3.1.52 (Recommended.)
PubMed references for 1.3.1.52
PubMed Central references for 1.3.1.52
Google Scholar references for 1.3.1.52
Komuniecki R, Fekete S, Thissen-Parra J (1985). "Purification and characterization of the 2-methyl branched-chain Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum". J. Biol. Chem. 260: 4770–7. PMID 3988734.
Komuniecki R, McCrury J, Thissen J, Rubin N (1989). "Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction". Biochim. Biophys. Acta. 975: 127–31. PMID 2736251.