Bis-gamma-glutamylcystine reductase
Bis-gamma-glutamylcystine reductase (EC 1.8.1.13) is an enzyme that catalyzes the chemical reaction
- 2 gamma-glutamylcysteine + NADP+ bis-gamma-glutamylcystine + NADPH + H+
bis-gamma-glutamylcystine reductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.8.1.13 | ||||||||
CAS no. | 117056-54-9 | ||||||||
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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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.
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