CoA-glutathione reductase

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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⁺ $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.8.1.10
BRENDA references for 1.8.1.10 (Recommended.)
PubMed references for 1.8.1.10
PubMed Central references for 1.8.1.10
Google Scholar references for 1.8.1.10
Ondarza RN, Abney R, Lopez-Colome AM (1969). "Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast". Biochim. Biophys. Acta. 191: 239–48. PMID 4390951.
Ondarza RN, Escamilla E, Gutierrez J, De la Chica G (1974). "CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity". Biochim. Biophys. Acta. 341: 162–71. PMID 4151341.
Carlberg I, Mannervik B (1977). "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: 268–74. PMID 334266.