Biology:Very-long-chain acyl-CoA dehydrogenase
From HandWiki
| Very-long-chain acyl-CoA dehydrogenase | |||||||||
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 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
This enzyme contains FAD as prosthetic group.
References
- ↑ "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. January 1992. doi:10.1016/S0021-9258(18)48390-1. PMID 1730632.
- ↑ "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. June 1995. doi:10.1172/JCI117947. PMID 7769092.
- ↑ "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. April 2008. doi:10.1074/jbc.M709135200. PMID 18227065.
External links
- Very-long-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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