| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.4 With a disulfide as acceptor |
| ID: | 1.8.4.3 |
|---|---|
| Description: | Glutathione--CoA-glutathione transhydrogenase. |
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 1.8.4.3 |
| BRENDA Enzyme Link: | BRENDA 1.8.4.3 |
| KEGG Enzyme Link: | KEGG1.8.4.3 |
| BioCyc Enzyme Link: | BioCyc 1.8.4.3 |
| ExPASy Enzyme Link: | ExPASy1.8.4.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.4.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.4.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.4.3 |
| IntEnz Enzyme Link: | IntEnz 1.8.4.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.4.3 |
| RHEA:13125 | CoA + glutathione disulfide = CoA-glutathione + glutathione |
| RULE(radius=1) | [*:1]-[S;H0;+0:2]-[S;H0;+0:3]-[*:4].[*:5]-[SH;+0:6]>>[*:5]-[S;H0;+0:6]-[S;H0;+0:3]-[*:4].[*:1]-[SH;+0:2] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Participation of the unsymmetrical disulfide of coenzyme A and glutathione in an enzymatic sulfhydryl-disulfide interchange. I. Partial purification and properties of the bovine kidney enzyme. | Chang SH, Wilken DR | 1966 Sep 25 | 5924646 |