| EC |
1.8.1.10 |
| Accepted name: |
CoA-glutathione reductase |
| Reaction: |
CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+ |
| Other name(s): |
coenzyme A glutathione disulfide reductase; NADPH-dependent coenzyme A-SS-glutathione reductase; coenzyme A disulfide-glutathione reductase; NADPH2:CoA-glutathione oxidoreductase |
| Systematic name: |
glutathione:NADP+ oxidoreductase (CoA-acylating) |
| Comments: |
A flavoprotein. The substrate is a mixed disulfide. May be identical to EC 1.8.1.9, thioredoxin-disulfide reductase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-33-0 |
| References: |
| 1. |
Ondarza, R.N., Abney, R. and López-Colomé, A.M. Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast. Biochim. Biophys. Acta 191 (1969) 239–248. [DOI] [PMID: 4390951] |
| 2. |
Ondarza, R.N., Escamilla, E., Gutierrez, J. and 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) 162–171. [DOI] [PMID: 4151341] |
| 3. |
Carlberg, I. and 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) 268–274. [DOI] [PMID: 334266] |
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| [EC 1.8.1.10 created 1972 as EC 1.6.4.6, transferred 2002 to EC 1.8.1.10] |
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