EC number:1.3.8.9
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.8 With a flavin as acceptor |
| ID: | 1.3.8.9 |
|---|---|
| Description: | Very-long-chain acyl-CoA dehydrogenase. |
| Cath: | 1.10.540.10; 1.20.140.10; 2.40.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.8.9 |
| BRENDA Enzyme Link: | BRENDA 1.3.8.9 |
| KEGG Enzyme Link: | KEGG1.3.8.9 |
| BioCyc Enzyme Link: | BioCyc 1.3.8.9 |
| ExPASy Enzyme Link: | ExPASy1.3.8.9 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.8.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.8.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.8.9 |
| IntEnz Enzyme Link: | IntEnz 1.3.8.9 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.8.9 |
| RHEA:19181 | a very-long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a very-long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein] |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]:[c;H0;+0:6]1:[n;H0;+0:7]:[*:8]:[*:9]:[n;H0;+0:10](-[*:11]):[c;H0;+0:12]-1:[n;H0;+0:13]:[*:14].[H+;H0:15]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[*:5]:[c;H0;+0:6]1:[c;H0;+0:12](:[nH;+0:13]:[*:14])-[N;H0;+0:10](-[*:11])-[*:9]:[*:8]-[NH;+0:7]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. | Aoyama T, Souri M, Ushikubo S, Kamijo T, Yamaguchi S, Kelley RI, Rhead WJ, Uetake K, Tanaka K, Hashimoto T | 1995 Jun | 7769092 |
| Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. | McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ | 2008 Apr 4 | 18227065 |
| Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain acyl-coenzyme A dehydrogenase. | Izai K, Uchida Y, Orii T, Yamamoto S, Hashimoto T | 1992 Jan 15 | 1730632 |