EC - Very-long-chain acyl-CoA dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
very-long-chain acyl-CoA dehydrogenase
Other name:
ACADVL (gene name)
Systematic name:
very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase




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, short-chain acyl-CoA dehydrogenase, EC, medium-chain acyl-CoA dehydrogenase, and EC, long-chain acyl-CoA dehydrogenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  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 created 1961 as EC, transferred 1964 to EC, part transferred 2012 to EC]