| Entry |
|
| Name |
CoA-glutathione reductase;
coenzyme A glutathione disulfide reductase;
NADPH-dependent coenzyme A-SS-glutathione reductase;
coenzyme A disulfide-glutathione reductase;
NADPH:CoA-glutathione oxidoreductase |
| Class |
Oxidoreductases;
Acting on a sulfur group of donors;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
glutathione:NADP+ oxidoreductase (CoA-acylating) |
| Reaction(IUBMB) |
CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+ [RN:R05714] |
| Reaction(KEGG) |
R05714;
(other) R00900
 |
| Substrate |
CoA [CPD:C00010];
glutathione [CPD:C00051];
NADP+ [CPD:C00006] |
| Product |
CoA-glutathione [CPD:C00920];
NADPH [CPD:C00005];
H+ [CPD:C00080] |
| Cofactor |
FAD [CPD:C00016] |
| Comment |
A flavoprotein. The substrate is a mixed disulfide. May be identical
to EC 1.8.1.9, thioredoxin-disulfide reductase. |
| Pathway |
PATH: ec00270 Cysteine and methionine metabolism |
Reference Authors Title
Journal Organism
|
1 [PMID:4390951]
Ondarza RN, Abney R, Lopez-Colome AM.
Characterization of a NADPH-dependent coenzyme A-SS-glutathione
reductase from yeast.
Biochim. Biophys. Acta. 191 (1969) 239-48.
Saccharomyces cerevisiae [GN:sce] |
Reference Authors Title
Journal Organism
|
2 [PMID:4151341]
Ondarza RN, Escamilla E, Gutierrez J, De la Chica G.
CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide
oxidoreductase activities in one protein entity.
Biochim. Biophys. Acta. 341 (1974) 162-71.
Rattus norvegicus [GN:rno] |
Reference Authors Title
Journal Organism
|
3 [PMID:334266]
Carlberg I, Mannervik B.
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.
Biochim. Biophys. Acta. 484 (1977) 268-74.
Saccharomyces cerevisiae [GN:sce] |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.8.1.10
IUBMB Enzyme Nomenclature: 1.8.1.10
ExPASy - ENZYME nomenclature database: 1.8.1.10
BRENDA, the Enzyme Database: 1.8.1.10
CAS: 37256-33-0 |