EC number:1.8.5.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.5 With a quinone or similar compound as acceptor |
| ID: | 1.8.5.1 |
|---|---|
| Description: | Glutathione dehydrogenase (ascorbate). |
| Cath: | 1.20.1050.10; 3.40.30.10; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.5.1 |
| BRENDA Enzyme Link: | BRENDA 1.8.5.1 |
| KEGG Enzyme Link: | KEGG1.8.5.1 |
| BioCyc Enzyme Link: | BioCyc 1.8.5.1 |
| ExPASy Enzyme Link: | ExPASy1.8.5.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.5.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.5.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.5.1 |
| IntEnz Enzyme Link: | IntEnz 1.8.5.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.5.1 |
| RHEA:24424 | 2 glutathione + L-dehydroascorbate = glutathione disulfide + L-ascorbate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:7]-[SH;+0:8].[*:9]-[SH;+0:10]>>[*:1]-[C;H0;+0:2](-[OH;+0:3])=[C;H0;+0:4](-[*:5])-[OH;+0:6].[*:7]-[S;H0;+0:8]-[S;H0;+0:10]-[*:9] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Oxidative stress in Caenorhabditis elegans: protective effects of the Omega class glutathione transferase (GSTO-1). | Burmeister C, Lüersen K, Heinick A, Hussein A, Domagalski M, Walter RD, Liebau E | 2008 Feb | 17901115 |
| The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin). | Washburn MP, Wells WW | 1999 Jan 5 | 9890907 |
| Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases. | Garcerá A, Barreto L, Piedrafita L, Tamarit J, Herrero E | 2006 Sep 1 | 16709151 |