Very-long-chain acyl-CoA dehydrogenase

Very-long-chain acyl-CoA dehydrogenase
Identifiers
EC number 1.3.8.9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Very-long-chain acyl-CoA dehydrogenase (EC 1.3.8.9, 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 \rightleftharpoons a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.

References

  1. Izai, K., Uchida, Y., Orii, T., Yamamoto, S. and 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. and 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. and 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.

External links

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