- References
- External links
| Name = Very-long-chain acyl-CoA dehydrogenase
| EC_number = 1.3.8.9
| CAS_number =
| IUBMB_EC_number = 1/3/8/9
| GO_code =
| image = 2uxw.jpg
| width = 270
| caption = Very long chain acyl-CoA dehydrogenase dimer, Human
}}Very-long-chain acyl-CoA dehydrogenase ({{EC number|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 flavoproteina very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
This enzyme contains FAD as prosthetic group.
References
1. ^{{cite journal | title = Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase |author1 = Izai, K. |author2 =Uchida, Y. |author3 =Orii, T. |author4 =Yamamoto, S. |author5 =Hashimoto, T. |journal = J. Biol. Chem. |year = 1992 |volume = 267 |pages = 1027–1033 |pmid = 1730632 |issue=2}}
2. ^{{cite journal | title = Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients |author1 = Aoyama, T. |author2 =Souri, M. |author3 =Ushikubo, S. |author4 =Kamijo, T. |author5 =Yamaguchi, S. |author6 =Kelley, R.I. |author7 =Rhead, W.J. |author8 =Uetake, K. |author9 =Tanaka, K. |author10 =Hashimoto, T. |journal = J. Clin. Invest. |year = 1995 |volume = 95 |pages = 2465–2473 |pmid = 7769092 |doi=10.1172/JCI117947 |issue=6 |pmc=295925}}
3. ^{{cite journal | title = Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase |author1 = McAndrew, R.P. |author2 =Wang, Y. |author3 =Mohsen, A.W. |author4 =He, M. |author5 =Vockley, J. |author6 =Kim, J.J. | journal = J. Biol. Chem. |year = 2008 |volume = 283 |pages = 9435–9443 |pmid = 18227065 |doi=10.1074/jbc.M709135200 |issue=14 |pmc=2431035}}
2. ^{{cite journal | title = Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients |author1 = Aoyama, T. |author2 =Souri, M. |author3 =Ushikubo, S. |author4 =Kamijo, T. |author5 =Yamaguchi, S. |author6 =Kelley, R.I. |author7 =Rhead, W.J. |author8 =Uetake, K. |author9 =Tanaka, K. |author10 =Hashimoto, T. |journal = J. Clin. Invest. |year = 1995 |volume = 95 |pages = 2465–2473 |pmid = 7769092 |doi=10.1172/JCI117947 |issue=6 |pmc=295925}}
3. ^{{cite journal | title = Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase |author1 = McAndrew, R.P. |author2 =Wang, Y. |author3 =Mohsen, A.W. |author4 =He, M. |author5 =Vockley, J. |author6 =Kim, J.J. | journal = J. Biol. Chem. |year = 2008 |volume = 283 |pages = 9435–9443 |pmid = 18227065 |doi=10.1074/jbc.M709135200 |issue=14 |pmc=2431035}}
External links
- {{MeshName|Very-long-chain+acyl-CoA+dehydrogenase}}
1 : EC 1.3.8