EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.1 With NAD+ or NADP+ as acceptor |
ID: | 1.8.1.13 |
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Description: | Bis-gamma-glutamylcystine reductase. |
Alternative Name: |
NADPH:bis-gamma-glutamylcysteine oxidoreductase. Bis-gamma-glutamylcystine reductase (NADPH). |
Cath: | 3.30.390.30; 3.50.50.60; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.8.1.13 |
BRENDA Enzyme Link: | BRENDA 1.8.1.13 |
KEGG Enzyme Link: | KEGG1.8.1.13 |
BioCyc Enzyme Link: | BioCyc 1.8.1.13 |
ExPASy Enzyme Link: | ExPASy1.8.1.13 |
EC2PDB Enzyme Link: | EC2PDB 1.8.1.13 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.13 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.13 |
IntEnz Enzyme Link: | IntEnz 1.8.1.13 |
MEDLINE Enzyme Link: | MEDLINE 1.8.1.13 |
RHEA:11980 | 2 L-gamma-glutamyl-L-cysteine + NADP(+) = bis-gamma-glutamylcystine + H(+) + NADPH |
RULE(radius=1) | [*:1]-[SH;+0:2].[*:3]-[SH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[S;H0;+0:2]-[S;H0;+0:4]-[*:3] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
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. | Sundquist AR, Fahey RC | 1988 Aug | 3136140 |
The function of gamma-glutamylcysteine and bis-gamma-glutamylcystine reductase in Halobacterium halobium. | Sundquist AR, Fahey RC | 1989 Jan 15 | 2910862 |
The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family. | Kim J, Copley SD | 2013 Apr 30 | 23560638 |