Very-long-chain acyl-CoA dehydrogenase

Very-long-chain acyl-CoA dehydrogenase

Very long chain acyl-CoA dehydrogenase dimer, Human

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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

\rightleftharpoons

a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.

References

^ 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.
^ 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.
^ 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.

External links

Very-long-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Oxidoreductases: CH–CH oxidoreductases (EC 1.3)
1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase
1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase
1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD
1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)