Biology:CoA-glutathione reductase
| CoA-glutathione reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.8.1.10 | ||||||||
| CAS number | 37256-33-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction
- CoA + glutathione + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] CoA-glutathione + NADPH + H+
The 3 substrates of this enzyme are CoA, glutathione, and NADP+, whereas its 3 products are CoA-glutathione, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutathione:NADP+ oxidoreductase (CoA-acylating). Other names in common use include coenzyme A glutathione disulfide reductase, NADPH-dependent coenzyme A-SS-glutathione reductase, coenzyme A disulfide-glutathione reductase, and NADPH:CoA-glutathione oxidoreductase. This enzyme participates in cysteine metabolism. It employs one cofactor, FAD.
References
- "Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast". Biochim. Biophys. Acta 191 (2): 239–48. 1969. doi:10.1016/0005-2744(69)90243-5. PMID 4390951.
- "CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity". Biochim. Biophys. Acta 341 (1): 162–71. 1974. doi:10.1016/0005-2744(74)90076-x. PMID 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". Biochim. Biophys. Acta 484 (2): 268–74. 1977. doi:10.1016/0005-2744(77)90083-3. PMID 334266.
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