Very-long-chain acyl-CoA dehydrogenase

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Very-long-chain acyl-CoA dehydrogenase
Very long chain acyl-CoA dehydrogenase dimer, Human
EC no.
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Very-long-chain acyl-CoA dehydrogenase (EC, ACADVL (gene).) is an enzyme with systematic name very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction

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

This enzyme contains FAD as prosthetic group.


  1. ^ Izai K, Uchida Y, Orii T, Yamamoto S, Hashimoto T (January 1992). "Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase". The Journal of Biological Chemistry. 267 (2): 1027–33. doi:10.1016/S0021-9258(18)48390-1. PMID 1730632.
  2. ^ Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T (June 1995). "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". The Journal of Clinical Investigation. 95 (6): 2465–73. doi:10.1172/JCI117947. PMC 295925. PMID 7769092.
  3. ^ McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ (April 2008). "Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase". The Journal of Biological Chemistry. 283 (14): 9435–43. doi:10.1074/jbc.M709135200. PMC 2431035. PMID 18227065.

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