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 number1.3.8.9
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. (1992). "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 (2): 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.; Hashimoto, T. (1995). "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients". J. Clin. Invest. 95 (6): 2465–2473. doi:10.1172/JCI117947. PMC 295925. PMID 7769092.
  3. ^ McAndrew, R.P.; Wang, Y.; Mohsen, A.W.; He, M.; Vockley, J.; Kim, J.J. (2008). "Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase". J. Biol. Chem. 283 (14): 9435–9443. doi:10.1074/jbc.M709135200. PMC 2431035. PMID 18227065.

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