IntEnz

EC 1.3.8.9 - Very-long-chain acyl-CoA dehydrogenase

IntEnz Enzyme Nomenclature
EC 1.3.8.9

Names

Reaction

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

Cofactor

• FAD

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. It's 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.

Links to other databases

References

1. 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 : 1027-1033 (1992). [PMID: 1730632]
2. Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R. I., Rhead, W. J., 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 : 2465-2473 (1995). [PMID: 7769092]
3. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., 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 : 9435-9443 (2008). [PMID: 18227065]

[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]