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Bis-gamma-glutamylcystine reductase (EC 1.8.1.13) is an enzyme that catalyzes the chemical reaction

2 gamma-glutamylcysteine + NADP ${\displaystyle \rightleftharpoons }$ bis-gamma-glutamylcystine + NADPH + H

Thus, the two substrates of this enzyme are gamma-glutamylcysteine and nicotinamide adenine dinucleotide phosphate ion, whereas its 3 products are bis-gamma-glutamylcystine, nicotinamide adenine dinucleotide phosphate, and hydrogen ion.

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 gamma-glutamylcysteine:NADP+ oxidoreductase. This enzyme is also called NADPH2:bis-gamma-glutamylcysteine oxidoreductase. This enzyme participates in glutathione metabolism.

References

• Sundquist AR, Fahey RC (1988). "The novel disulfide reductase bis-gamma-glutamylcystine reductase and dihydrolipoamide dehydrogenase from Halobacterium halobium: purification by immobilized-metal-ion affinity chromatography and properties of the enzymes". J. Bacteriol. 170 (8): 3459–67. PMC 211315. PMID 3136140.
• Sundquist AR, Fahey RC (1989). "The function of gamma-glutamylcysteine and bis-gamma-glutamylcystine reductase in Halobacterium halobium". J. Biol. Chem. 264 (2): 719–25. PMID 2910862.

• Biology

• EC 1.8.1
• NADPH-dependent enzymes
• Enzymes of unknown structure