Very-long-chain acyl-CoA dehydrogenase

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Very-long-chain acyl-CoA dehydrogenase
2uxw.jpg
Very long chain acyl-CoA dehydrogenase dimer, Human
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 a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.

References[edit]

  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 295925Freely accessible. 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 2431035Freely accessible. PMID 18227065. 

External links[edit]