Enzyme

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     1. Oxidoreductases
        1.8 Acting on a sulfur group of donors
            1.8.1 With NAD+ or NADP+ as acceptor
ID:1.8.1.7
Description:Glutathione-disulfide reductase.
Alternative Name: NADPH:oxidized-glutathione oxidoreductase.
NADPH-GSSG reductase.
NADPH-glutathione reductase.
GSSG reductase.
GSH reductase.
Glutathione S-reductase.
Glutathione reductase (NADPH).
Glutathione reductase.
Prosite: PDOC00073;
PDB:
PDBScop
Cath: 3.30.390.30; 3.50.50.60;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.8.1.7
BRENDA Enzyme Link: BRENDA 1.8.1.7
KEGG Enzyme Link: KEGG1.8.1.7
BioCyc Enzyme Link: BioCyc 1.8.1.7
ExPASy Enzyme Link: ExPASy1.8.1.7
EC2PDB Enzyme Link: EC2PDB 1.8.1.7
ExplorEnz Enzyme Link: ExplorEnz 1.8.1.7
PRIAM enzyme-specific profiles Link: PRIAM 1.8.1.7
IntEnz Enzyme Link: IntEnz 1.8.1.7
MEDLINE Enzyme Link: MEDLINE 1.8.1.7
MSA:

1.8.1.7;

Phylogenetic Tree:

1.8.1.7;

Uniprot:
M-CSA:
RHEA:11740 2 glutathione + NADP(+) = glutathione disulfide + 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 More

References

TitleAuthorsDatePubMed ID
The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.Pai EF, Schulz GE1983 Feb 106822532
Refined structure of glutathione reductase at 1.54 A resolution.Karplus PA, Schulz GE1987 Jun 53656429
Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.Karplus PA, Schulz GE1989 Nov 52585516
The glutathione reductase GSR-1 determines stress tolerance and longevity in Caenorhabditis elegans.Lüersen K, Stegehake D, Daniel J, Drescher M, Ajonina I, Ajonina C, Hertel P, Woltersdorf C, Liebau E201323593298
Human erythrocyte glutathione reductase: chemical mechanism and structure of the transition state for hydride transfer.Sweet WL, Blanchard JS1991 Sep 31888731
Catalytic cycle of human glutathione reductase near 1 A resolution.Berkholz DS, Faber HR, Savvides SN, Karplus PA2008 Oct 318638483
Purification and characterization of glutathione reductase from Rhodospirillum rubrum.Libreros-Minotta CA, Pardo JP, Mendoza-Hernández G, Rendón JL1992 Oct1524433
Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme.Bohme CC, Arscott LD, Becker K, Schirmer RH, Williams CH Jr2000 Dec 110969088