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 |
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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 |