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In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5) is an enzyme that catalyzes the chemical reaction

2-methylbutanoyl-CoA + electron transfer flavoprotein ${\displaystyle \rightleftharpoons }$ 2-methylcrotonoyl-CoA + reduced electron transfer flavoprotein + H

Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and an electron transfer flavoprotein, whereas its 3 products are 2-methylcrotonoyl-CoA, reduced electron transfer flavoprotein, and H.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donors with flavin as acceptor. The systematic name of this enzyme class is 2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase . This enzyme participates in the degradation of isoleucine. It employs one cofactor, FAD.

References

• 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 (8): 4770–7. doi:10.1016/S0021-9258(18)89138-4. 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 (1): 127–31. doi:10.1016/s0005-2728(89)80210-5. PMID 2736251.

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