CoA-glutathione reductase
Enzyme / From Wikipedia, the free encyclopedia
In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction
- CoA + glutathione + NADP+ CoA-glutathione + NADPH + H+
CoA-glutathione reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.1.10 | ||||||||
CAS no. | 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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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.