EC number:1.8.1.10
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.8.1.10 |
|---|---|
| Description: | CoA-glutathione reductase. |
| Alternative Name: |
NADPH:CoA-glutathione oxidoreductase. NADPH-dependent coenzyme A-SS-glutathione reductase. Coenzyme A glutathione disulfide reductase. Coenzyme A disulfide-glutathione reductase. CoA-glutathione reductase (NADPH). |
| Cath: | 3.30.390.30; 3.50.50.60; 3.40.30.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.1.10 |
| BRENDA Enzyme Link: | BRENDA 1.8.1.10 |
| KEGG Enzyme Link: | KEGG1.8.1.10 |
| BioCyc Enzyme Link: | BioCyc 1.8.1.10 |
| ExPASy Enzyme Link: | ExPASy1.8.1.10 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.1.10 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.10 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.10 |
| IntEnz Enzyme Link: | IntEnz 1.8.1.10 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.1.10 |
| RHEA:14617 | CoA + glutathione + NADP(+) = CoA-glutathione + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[SH;+0:2].[*:3]-[SH;+0:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1.[*:3]-[S;H0;+0:4]-[S;H0;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast. | Ondarza RN, Abney R, López-Colomé AM | 1969 Nov 4 | 4390951 |
| CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity. | Ondarza RN, Escamilla E, Gutiérrez J, De la Chica G | 1974 Mar 21 | 4151341 |
| Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione. | Carlberg I, Mannervik B | 1977 Oct 13 | 334266 |