| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.8 With a flavin as acceptor |
| ID: | 1.3.8.6 | ||
|---|---|---|---|
| Description: | Glutaryl-CoA dehydrogenase (ETF). | ||
| Alternative Name: |
Glutaryl-CoA dehydrogenase. | ||
| Prosite: | PDOC00070; | ||
| PDB: |
|
||
| Cath: | 1.10.540.10; 1.20.140.10; 2.40.110.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.3.8.6 |
| BRENDA Enzyme Link: | BRENDA 1.3.8.6 |
| KEGG Enzyme Link: | KEGG1.3.8.6 |
| BioCyc Enzyme Link: | BioCyc 1.3.8.6 |
| ExPASy Enzyme Link: | ExPASy1.3.8.6 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.8.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.8.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.8.6 |
| IntEnz Enzyme Link: | IntEnz 1.3.8.6 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.8.6 |
| RHEA:13389 | glutaryl-CoA + 2 H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer flavoprotein] |
| RULE(radius=1) | [*:1]:[c;H0;+0:2]1:[n;H0;+0:3]:[*:4]:[*:5]:[n;H0;+0:6](-[*:7]):[c;H0;+0:8]-1:[n;H0;+0:9]:[*:10].[*:11]=[C;H0;+0:12](-[OH;+0:13])-[CH2;+0:14]-[CH2;+0:15]-[CH2;+0:16]-[*:17].[H+;H0:18].[H+;H0:19]>>[*:17]-[CH;+0:16]=[CH;+0:15]-[CH3;+0:14].[*:1]:[c;H0;+0:2]1:[c;H0;+0:8](:[nH;+0:9]:[*:10])-[N;H0;+0:6](-[*:7])-[*:5]:[*:4]-[NH;+0:3]-1.[*:11]=[C;H0;+0:12]=[O;H0;+0:13] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate. | Härtel U, Eckel E, Koch J, Fuchs G, Linder D, Buckel W | 1993 | 8439237 |
| Mammalian metabolism of glutaric acid. | Besrat A, Polan CE, Henderson LM | 1969 Mar 25 | 4304226 |
| Kinetic mechanism of glutaryl-CoA dehydrogenase. | Rao KS, Albro M, Dwyer TM, Frerman FE | 2006 Dec 26 | 17176108 |
| The functions of the flavin contact residues, alphaArg249 and betaTyr16, in human electron transfer flavoprotein. | Dwyer TM, Zhang L, Muller M, Marrugo F, Frerman F | 1999 Aug 17 | 10446367 |