Reaction: a very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Glossary: a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.
Other name(s): ACADVL (gene name).
Systematic name: very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-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 . cf. EC 126.96.36.199, short-chain acyl-CoA dehydrogenase, EC 188.8.131.52, medium-chain acyl-CoA dehydrogenase, and EC 184.108.40.206, long-chain acyl-CoA dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
1. Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and Hashimoto, T. Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. J. Biol. Chem. 267 (1992) 1027-1033. [PMID: 1730632]
2. Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K. and Hashimoto, T. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. J. Clin. Invest. 95 (1995) 2465-2473. [PMID: 7769092]
3. McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J. and Kim, J.J. Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. J. Biol. Chem. 283 (2008) 9435-9443. [PMID: 18227065]