EC |
1.8.1.13 |
Accepted name: |
bis-γ-glutamylcystine reductase |
Reaction: |
2 γ-glutamylcysteine + NADP+ = bis-γ-glutamylcystine + NADPH + H+ |
Other name(s): |
NADPH2:bis-γ-glutamylcysteine oxidoreductase; GSR |
Systematic name: |
γ-glutamylcysteine:NADP+ oxidoreductase |
Comments: |
Contains FAD. The enzyme, which is found only in halobacteria, maintains the concentration of γ-glutamylcysteine, the major low molecular weight thiol in halobacteria. Not identical with EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.14 (CoA-disulfide reductase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117056-54-9 |
References: |
1. |
Sundquist, A.R. and Fahey, R.C. The novel disulfide reductase bis-γ-glutamylcystine reductase and dihydrolipoamide dehydrogenase from Halobacterium halobium: purification by immobilized-metal-ion affinity chromatography and properties of the enzymes. J. Bacteriol. 170 (1988) 3459–3467. [DOI] [PMID: 3136140] |
2. |
Sundquist, A.R. and Fahey, R.C. The function of γ-glutamylcysteine and bis-γ-glutamylcystine reductase in Halobacterium halobium. J. Biol. Chem. 264 (1989) 719–725. [PMID: 2910862] |
3. |
Kim, J. and Copley, S.D. The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family. Biochemistry 52 (2013) 2905–2913. [DOI] [PMID: 23560638] |
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[EC 1.8.1.13 created 1992 as EC 1.6.4.9, transferred 2002 to EC 1.8.1.13, modified 2013] |
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