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

  1. References

{{enzyme
| Name = 2-methyl-branched-chain-enoyl-CoA reductase
| EC_number = 1.3.8.5
| CAS_number = 122320-06-3
| IUBMB_EC_number = 1/3/8/5
| GO_code = 0047119
| image =
| width =
| caption =
}}

In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase ({{EC number|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

  • {{cite journal |vauthors=Komuniecki R, Fekete S, Thissen-Parra J | date = 1985 | title = 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 | journal = J. Biol. Chem. | volume = 260 | pages = 4770–7 | pmid = 3988734 | issue = 8 }}
  • {{cite journal |vauthors=Komuniecki R, McCrury J, Thissen J, Rubin N | date = 1989 | title = Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction | journal = Biochim. Biophys. Acta | volume = 975 | pages = 127–31 | pmid = 2736251 | issue = 1 | doi=10.1016/s0005-2728(89)80210-5}}
{{CH-CH oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.3-enzyme-stub}}

3 : EC 1.3.8|Flavin enzymes|Enzymes of unknown structure

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