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

Class of enzymes 2-methyl-branched-chain-enoyl-CoA reductase 1.3.8.5 122320-06-3 0047119 In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase (1.3.8.5) is an enzyme that catalyzes the chemical reaction 2-methylbutanoyl-CoA + electron transfer flavoprotein 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 1 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 3988734 8 10.1016/S0021-9258(18)89138-4 free 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 2736251 1 10.1016/s0005-2728(89)80210-5 Biology no Category:EC 1.3.8 Category:Flavoproteins Category:Enzymes of unknown structure