Jump to content

Very-long-chain acyl-CoA dehydrogenase

From Wikipedia, the free encyclopedia
The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.
Very-long-chain acyl-CoA dehydrogenase
Very long chain acyl-CoA dehydrogenase dimer, Human
Identifiers
EC no.1.3.8.9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  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.