Bis-gamma-glutamylcystine reductase
| bis-gamma-glutamylcystine reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
Bis-gamma-glutamylcystine reductase (EC 1.8.1.13) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are bis-γ-glutamylcystine, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and a proton. Its products are γ-L-Glutamyl-L-cysteine and oxidised NADP+.[1][2][3]
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
- ^ Enzyme 1.8.1.13 at KEGG Pathway Database.
- ^ 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. doi:10.1128/jb.170.8.3459-3467.1988. 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. doi:10.1016/S0021-9258(19)85002-0. PMID 2910862.