Oxidoreductases;
Acting on the CH-CH group of donors;
With a flavin as acceptor
BRITE hierarchy

very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase

a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

(other) R01279 R03990
Reaction

very-long-chain acyl-CoA [CPD:C20876];
electron-transfer flavoprotein [CPD:C04253]

Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase [1]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase.

EC 1.3.8.9 created 1961 as EC 1.3.2.2, transferred 1964 to EC 1.3.99.3, part transferred 2012 to EC 1.3.8.9

1  [PMID:1730632]

Izai K, Uchida Y, Orii T, Yamamoto S, Hashimoto T

Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase.

J Biol Chem 267:1027-33 (1992)

[rno:25363]

2  [PMID:7769092]

Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T

Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients.

J Clin Invest 95:2465-73 (1995)
DOI:10.1172/JCI117947

[hsa:37]

3  [PMID:18227065]

McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ

Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.

J Biol Chem 283:9435-43 (2008)
DOI:10.1074/jbc.M709135200

[hsa:37]