DB code: T00213

CATH domain 3.50.50.60 : FAD/NAD(P)-binding domain Catalytic domain
3.50.50.60 : FAD/NAD(P)-binding domain Catalytic domain
3.30.390.30 : Enolase-like; domain 1 Catalytic domain
E.C. 1.8.1.7
CSA 1get
M-CSA 1get
MACiE M0006

CATH domain Related DB codes (homologues)
3.50.50.60 : FAD/NAD(P)-binding domain M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00017 T00025 T00211 T00233 T00242
3.30.390.30 : Enolase-like; domain 1 M00163 T00017 T00233 T00242

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P06715 Glutathione reductase
GRase
GR
EC 1.8.1.7
NP_417957.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491935.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00070 (Pyr_redox)
PF07992 (Pyr_redox_2)
PF02852 (Pyr_redox_dim)
[Graphical View]
P41921 Glutathione reductase
GRase
GR
EC 1.8.1.7
NP_015234.1 (Protein)
NM_001183905.1 (DNA/RNA sequence)
PF00070 (Pyr_redox)
PF07992 (Pyr_redox_2)
PF02852 (Pyr_redox_dim)
[Graphical View]
Q94655 Glutathione reductase
GRase
GR
EC 1.8.1.7
PF00070 (Pyr_redox)
PF07992 (Pyr_redox_2)
PF02852 (Pyr_redox_dim)
[Graphical View]
P00390 Glutathione reductase, mitochondrial
GRase
GR
EC 1.8.1.7
NP_000628.2 (Protein)
NM_000637.3 (DNA/RNA sequence)
NP_001182031.1 (Protein)
NM_001195102.1 (DNA/RNA sequence)
NP_001182032.1 (Protein)
NM_001195103.1 (DNA/RNA sequence)
NP_001182033.1 (Protein)
NM_001195104.1 (DNA/RNA sequence)
PF00070 (Pyr_redox)
PF07992 (Pyr_redox_2)
PF02852 (Pyr_redox_dim)
[Graphical View]

KEGG enzyme name
glutathione-disulfide reductase
glutathione reductase
glutathione reductase (NADPH)
NADPH-glutathione reductase
GSH reductase
GSSG reductase
NADPH-GSSG reductase
glutathione S-reductase
NADPH:oxidized-glutathione oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P06715 GSHR_ECOLI 2 glutathione + NADP(+) = glutathione disulfide + NADPH. Homodimer. Cytoplasm. Binds 1 FAD per subunit.
P41921 GSHR_YEAST 2 glutathione + NADP(+) = glutathione disulfide + NADPH. Cytoplasm (By similarity). Binds 1 FAD per subunit (By similarity).
Q94655 GSHR_PLAFK 2 glutathione + NADP(+) = glutathione disulfide + NADPH. Homodimer. Cytoplasm. Binds 1 FAD per subunit (By similarity).
P00390 GSHR_HUMAN 2 glutathione + NADP(+) = glutathione disulfide + NADPH. Homodimer, disulfide-linked. Mitochondrion. Cytoplasm. Binds 1 FAD per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00480 Glutathione metabolism
MAP00251 Glutamate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00127 C00005 C00080 C00051 C00006
E.C.
Compound FAD Oxidized glutathione NADPH H+ Glutathione NADP+ glutathione-covalently-bound to Cys
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amino acids,carboxyl group,peptide/protein,disulfide bond amide group,amine group,nucleotide others amino acids,carboxyl group,peptide/protein,sulfhydryl group amide group,amine group,nucleotide
ChEBI 16238
17858
16474
15378
16856
18009
PubChem 643975
65359
11215652
5884
1038
25246407
124886
5886
1gerA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1gerB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1gesA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1gesB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1getA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1getB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1geuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1geuB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
2hqmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
2hqmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1onfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1bwcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Analogue:AJ3 Unbound Unbound
1dncA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-bound:GTT-CYS_58
1graA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:GSH-GSH Unbound Unbound Unbound Unbound
1grbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1greA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Bound:GSH_482 Unbound Intermediate-bound:GSH_481-CYS_58
1grfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-analogue:ACM-CYS_58
1grgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-analogue:CEC-CYS_58
1grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
1gsnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-bound:GTT-CYS_58
1xanA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
2aaqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
2gh5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-analogue:ELI-CYS_58
2gh5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-analogue:ELI-CYS_58
2grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Bound:GDS Unbound Unbound Unbound Unbound
3grsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Unbound
3grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Analogue:TS2 Unbound Unbound Unbound Unbound
4gr1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Analogue:RGS Unbound Unbound Unbound Unbound
4grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound Intermediate-analogue:GCG-CYS_58
5grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Analogue:TS4 Unbound Unbound Unbound Unbound
1gerA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gerB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gesA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gesB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1getA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Unbound
1getB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Bound:NAP Unbound
1geuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:NAD Unbound
1geuB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:NAD Unbound
2hqmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2hqmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1onfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1bwcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1dncA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1graA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Analogue:NDP Unbound Unbound Unbound
1grbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NDP Unbound Analogue:NAD Unbound
1greA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gsnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xanA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aaqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2gh5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2gh5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3grsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4gr1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
5grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gerA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gerB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gesA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gesB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1getA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1getB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1geuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1geuB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2hqmA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2hqmB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1onfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1bwcA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1dncA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1graA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grbA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1greA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grgA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gsnA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xanA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aaqA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2gh5A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2gh5B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3grsA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4gr1A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
4grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
5grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;2grt & Swiss-prot;P06715, P00390 & literature [7], [9], [16], [39], [46]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1gerA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 disulfide bonded/oxidized form C42-C47
1gerB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 disulfide bonded/oxidized form C42-C47
1gesA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 disulfide bonded/oxidized form C42-C47
1gesB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 disulfide bonded/oxidized form C42-C47
1getA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 reduced form C42, C47
1getB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 reduced form C42, C47
1geuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 reduced form C42, C47
1geuB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 42;CYS 47;LYS 50 reduced form C42, C47
2hqmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 61;CYS 66;LYS 69 disulfide bonded/oxidized form C61-C66
2hqmB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 61;CYS 66;LYS 69 disulfide bonded/oxidized form C61-C66
1onfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 39;CYS 44;LYS 47 reduced form C39, C44
1bwcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 disulfide bonded/oxidized form C58-C63
1dncA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58; ;LYS 66 CSD 63(sulfinylated) modified C63
1graA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 disulfide bonded/oxidized form C58-C63
1grbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 reduced form C58, C63
1greA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66
1grfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66
1grgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66
1grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
1gsnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58; ;LYS 66 CSO 63(sulfenylated)
1xanA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 disulfide bonded/oxidized form C58-C63
2aaqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 reduced form C58, C63
2gh5A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66
2gh5B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66
2grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
3grsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 disulfide bonded/oxidized form C58-C63
3grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
4gr1A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 disulfide bonded/oxidized form C58-C63
4grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 mutant A34E, R37W
5grtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 58;CYS 63;LYS 66 mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
1gerA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181
1gerB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181
1gesA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181 mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
1gesB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181 mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
1getA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181
1getB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181
1geuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181 mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
1geuB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 177;GLU 181 mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
2hqmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 207;GLU 211
2hqmB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 207;GLU 211
1onfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 185;GLU 189
1bwcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1dncA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1graA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1grbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1greA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1grfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1grgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1gsnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201 CSO 234(sulfenylated);CSO 284(sulfenylated)
1xanA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
2aaqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
2gh5A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
2gh5B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
2grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
3grsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
3grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
4gr1A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
4grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
5grtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 197;GLU 201
1gerA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1gerB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1gesA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1gesB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1getA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1getB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1geuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
1geuB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 439;GLU 444
2hqmA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 472;GLU 477
2hqmB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 472;GLU 477
1onfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 484;GLU 489
1bwcA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1dncA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1graA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1grbA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1greA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1grfA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1grgA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
1gsnA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472 CSO 423(sulfenylated)
1xanA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
2aaqA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
2gh5A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
2gh5B03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
2grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
3grsA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
3grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
4gr1A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
4grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472
5grtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 467;GLU 472

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.301-304
[3]
Fig.5, p.1754-1757
[4]
Fig.6, p.376-377
[5]
p.495
[7]
p.342-343
[9]
p.725-728
[11]
Fig.1, p.315
[13]
Fig.1, p.9602-9603
[16]
Fig.1, p.175-179
[17]
Fig.6, p.4028-4029
[40]
p.13972-13975, p.13976-13977
[48]
Scheme 3
[53]
p.900
[55]
p.10784-10785, Scheme 1, Scheme 2

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS) OF 45-522
Medline ID 82145544
PubMed ID 7334521
Journal J Mol Biol
Year 1981
Volume 152
Pages 763-82
Authors Thieme R, Pai EF, Schirmer RH, Schulz GE
Title Three-dimensional structure of glutathione reductase at 2 A resolution.
Related PDB
Related UniProtKB P00390
[2]
Resource
Comments
Medline ID
PubMed ID 7175934
Journal J Mol Biol
Year 1982
Volume 160
Pages 287-308
Authors Schulz GE, Schirmer RH, Pai EF
Title FAD-binding site of glutathione reductase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6822532
Journal J Biol Chem
Year 1983
Volume 258
Pages 1752-7
Authors Pai EF, Schulz GE
Title The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6697994
Journal Eur J Biochem
Year 1984
Volume 138
Pages 373-8
Authors Bilzer M, Krauth-Siegel RL, Schirmer RH, Akerboom TP, Sies H, Schulz GE
Title Interaction of a glutathione S-conjugate with glutathione reductase. Kinetic and X-ray crystallographic studies.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 6546954
Journal J Mol Biol
Year 1984
Volume 174
Pages 483-96
Authors Rice DW, Schulz GE, Guest JR
Title Structural relationship between glutathione reductase and lipoamide dehydrogenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 3885856
Journal Arch Biochem Biophys
Year 1985
Volume 238
Pages 213-8
Authors Huber PW, Brandt KG
Title Kinetic studies of the reduction of yeast glutathione reductase by reduced nicotinamide hypoxanthine dinucleotide phosphate.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 3987692
Journal Eur J Biochem
Year 1985
Volume 148
Pages 335-44
Authors Krauth-Siegel RL, Schirmer RH, Ghisla S
Title FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 3581436
Journal Cell Biochem Funct
Year 1987
Volume 5
Pages 79-95
Authors Rosemeyer MA
Title The biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 45-522
Medline ID 88011277
PubMed ID 3656429
Journal J Mol Biol
Year 1987
Volume 195
Pages 701-29
Authors Karplus PA, Schulz GE
Title Refined structure of glutathione reductase at 1.54 A resolution.
Related PDB 3grs
Related UniProtKB P00390
[10]
Resource
Comments
Medline ID
PubMed ID 2844232
Journal Biochemistry
Year 1988
Volume 27
Pages 4465-74
Authors Pai EF, Karplus PA, Schulz GE
Title Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 3338461
Journal Eur J Biochem
Year 1988
Volume 171
Pages 193-8
Authors Karplus PA, Krauth-Siegel RL, Schirmer RH, Schulz GE
Title Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 2666188
Journal Biochem Soc Trans
Year 1989
Volume 17
Pages 315-7
Authors Krauth-Siegel RL, Jockers-Scherubl MC, Becker K, Schirmer RH
Title NADPH-dependent disulphide reductases.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 2558727
Journal Biochemistry
Year 1989
Volume 28
Pages 9602-7
Authors Deonarain MP, Berry A, Scrutton NS, Perham RN
Title Alternative proton donors/acceptors in the catalytic mechanism of the glutathione reductase of Escherichia coli: the role of histidine-439 and tyrosine-99.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 2647141
Journal Biochim Biophys Acta
Year 1989
Volume 973
Pages 399-404
Authors Cenas NK, Rakauskiene GA, Kulys JJ
Title One- and two-electron reduction of quinones by glutathione reductase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 2912729
Journal Eur J Biochem
Year 1989
Volume 178
Pages 693-703
Authors Karplus PA, Pai EF, Schulz GE
Title A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution.
Related PDB
Related UniProtKB
[16]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2585516
Journal J Mol Biol
Year 1989
Volume 210
Pages 163-80
Authors Karplus PA, Schulz GE
Title Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.
Related PDB 1gra 1grb 1gre 1grf 1grg
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 2354175
Journal Biochemistry
Year 1990
Volume 29
Pages 4022-30
Authors Janes W, Schulz GE
Title Role of the charged groups of glutathione disulfide in the catalysis of glutathione reductase: crystallographic and kinetic studies with synthetic analogues.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 2176163
Journal FEBS Lett
Year 1990
Volume 276
Pages 189-91
Authors Shi XL, Dalal NS
Title NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2355009
Journal J Biol Chem
Year 1990
Volume 265
Pages 10443-5
Authors Janes W, Schulz GE
Title The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
Related PDB 4gr1
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2059620
Journal Biochemistry
Year 1991
Volume 30
Pages 6124-7
Authors Bradley M, Bucheler US, Walsh CT
Title Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase.
Related PDB 3grt
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 2065668
Journal Eur J Biochem
Year 1991
Volume 199
Pages 133-8
Authors Ermler U, Ghisla S, Massey V, Schulz GE
Title Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 1880807
Journal J Mol Biol
Year 1991
Volume 220
Pages 975-94
Authors Mattevi A, Schierbeek AJ, Hol WG
Title Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 2067578
Journal Nature
Year 1991
Volume 352
Pages 172-4
Authors Kuriyan J, Krishna TS, Wong L, Guenther B, Pahler A, Williams CH Jr, Model P
Title Convergent evolution of similar function in two structurally divergent enzymes.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 1924337
Journal Proc Natl Acad Sci U S A
Year 1991
Volume 88
Pages 8769-73
Authors Henderson GB, Murgolo NJ, Kuriyan J, Osapay K, Kominos D, Berry A, Scrutton NS, Hinchliffe NW, Perham RN, Cerami A
Title Engineering the substrate specificity of glutathione reductase toward that of trypanothione reduction.
Related PDB
Related UniProtKB
[25]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
Medline ID 91172742
PubMed ID 2006135
Journal Proteins
Year 1991
Volume 9
Pages 174-9
Authors Ermler U, Schulz GE
Title The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution.
Related PDB
Related UniProtKB P06715
[26]
Resource
Comments
Medline ID
PubMed ID 1524433
Journal Arch Biochem Biophys
Year 1992
Volume 298
Pages 247-53
Authors Libreros-Minotta CA, Pardo JP, Mendoza-Hernandez G, Rendon JL
Title Purification and characterization of glutathione reductase from Rhodospirillum rubrum.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 8510142
Journal J Mol Biol
Year 1993
Volume 231
Pages 191-5
Authors Mittl PR, Berry A, Scrutton NS, Perham RN, Schulz GE
Title Structural differences between wild-type NADP-dependent glutathione reductase from Escherichia coli and a redesigned NAD-dependent mutant.
Related PDB
Related UniProtKB
[28]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7833810
Journal Protein Sci
Year 1994
Volume 3
Pages 1504-14
Authors Mittl PR, Berry A, Scrutton NS, Perham RN, Schulz GE
Title Anatomy of an engineered NAD-binding site.
Related PDB 1ges 1get 1geu
Related UniProtKB
[29]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS)
Medline ID 94339840
PubMed ID 8061609
Journal Protein Sci
Year 1994
Volume 3
Pages 799-809
Authors Mittl PR, Schulz GE
Title Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.
Related PDB 1ger
Related UniProtKB P06715
[30]
Resource
Comments
Medline ID
PubMed ID 8526866
Journal Biochem J
Year 1995
Volume 312
Pages 527-33
Authors Bashir A, Perham RN, Scrutton NS, Berry A
Title Altering kinetic mechanism and enzyme stability by mutagenesis of the dimer interface of glutathione reductase.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 7499374
Journal J Biol Chem
Year 1995
Volume 270
Pages 28586-94
Authors Murthy YV, Massey V
Title Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 8739033
Journal Biochem Mol Biol Int
Year 1996
Volume 38
Pages 1117-26
Authors Paulikova H, Petrickova I, Antalik M, Podhradsky D
Title Effect of heparin and dextran sulfate on the activity of glutathione reductase from yeast.
Related PDB
Related UniProtKB
[33]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8626496
Journal J Biol Chem
Year 1996
Volume 271
Pages 8101-7
Authors Savvides SN, Karplus PA
Title Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor.
Related PDB 1xan
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 8691487
Journal J Med Chem
Year 1996
Volume 39
Pages 1549-54
Authors Schonleben-Janas A, Kirsch P, Mittl PR, Schirmer RH, Krauth-Siegel RL
Title Inhibition of human glutathione reductase by 10-arylisoalloxazines: crystalline, kinetic, and electrochemical studies.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 8631352
Journal Eur J Biochem
Year 1996
Volume 235
Pages 345-50
Authors Krauth-Siegel RL, M?ller JG, Lottspeich F, Schirmer RH
Title Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria.
Related PDB
Related UniProtKB Q94655
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9174360
Journal Biochemistry
Year 1997
Volume 36
Pages 6437-47
Authors Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF
Title Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Related PDB 1grt 2grt 4grt 5grt
Related UniProtKB
[37]
Resource
Comments NMR structure
Medline ID
PubMed ID 9151953
Journal Eur J Biochem
Year 1997
Volume 245
Pages 273-82
Authors Nordhoff A, Tziatzios C, van den Broek JA, Schott MK, Kalbitzer HR, Becker K, Schubert D, Schirmer RH
Title Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors.
Related PDB 1alg
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 9268306
Journal J Biol Chem
Year 1997
Volume 272
Pages 21767-73
Authors Boese M, Keese MA, Becker K, Busse R, Mulsch A
Title Inhibition of glutathione reductase by dinitrosyl-iron-dithiolate complex.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 9247856
Journal J Enzyme Inhib
Year 1997
Volume 12
Pages 143-54
Authors Pandey A, Iyengar L, Katiyar SS
Title Modification of an essential amino group of glutathione reductase from yeast by pyridoxal 5'-phosphate.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 9760231
Journal Biochemistry
Year 1998
Volume 37
Pages 13968-77
Authors Krauth-Siegel RL, Arscott LD, Schonleben-Janas A, Schirmer RH, Williams CH Jr
Title Role of active site tyrosine residues in catalysis by human glutathione reductase.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 9799522
Journal Biochemistry
Year 1998
Volume 37
Pages 15575-82
Authors Veine DM, Arscott LD, Williams CH Jr
Title Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD+/NADH redox couple: enzyme forms active in catalysis.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 9545063
Journal Biophys J
Year 1998
Volume 74
Pages 2046-58
Authors van den Berg PA, van Hoek A, Walentas CD, Perham RN, Visser AJ
Title Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 9535831
Journal J Biol Chem
Year 1998
Volume 273
Pages 8581-91
Authors Zhong L, Arn-er ES, Ljung J, Aslund F, Holmgren A
Title Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue.
Related PDB
Related UniProtKB
[44]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9546215
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 267-71
Authors Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA
Title Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers.
Related PDB 1dnc 1gsn
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 10413499
Journal Biochemistry
Year 1999
Volume 38
Pages 9254-63
Authors Danielson UH, Jiang F, Hansson LO, Mannervik B
Title Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 10094686
Journal J Bacteriol
Year 1999
Volume 181
Pages 2094-101
Authors van Hylckama Vlieg JE, Kingma J, Kruizinga W, Janssen DB
Title Purification of a glutathione S-transferase and a glutathione conjugate-specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45.
Related PDB
Related UniProtKB
[47]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9986706
Journal J Med Chem
Year 1999
Volume 42
Pages 364-72
Authors Gallwitz H, Bonse S, Martinez-Cruz A, Schlichting I, Schumacher K, Krauth-Siegel RL
Title Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies.
Related PDB 1bwc
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 10769127
Journal Biochemistry
Year 2000
Volume 39
Pages 4711-21
Authors Arscott LD, Veine DM, Williams CH Jr
Title Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell.
Related PDB
Related UniProtKB
[49]
Resource
Comments
Medline ID
PubMed ID 10779594
Journal Mol Biochem Parasitol
Year 2000
Volume 107
Pages 169-79
Authors Gilberger TW, Schirmer RH, Walter RD, Muller S
Title Deletion of the parasite-specific insertions and mutation of the catalytic triad in glutathione reductase from chloroquine-sensitive Plasmodium falciparum 3D7.
Related PDB
Related UniProtKB
[50]
Resource
Comments
Medline ID
PubMed ID 11370850
Journal Arch Biochem Biophys
Year 2001
Volume 387
Pages 265-72
Authors Rendon JL, Mendoza-Hernandez G
Title Unfolding kinetics of glutathione reductase from cyanobacterium Spirulina maxima.
Related PDB
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 11705998
Journal J Biol Chem
Year 2002
Volume 277
Pages 2779-84
Authors Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH
Title Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite.
Related PDB
Related UniProtKB
[52]
Resource
Comments
Medline ID
PubMed ID 12111385
Journal J Mol Model (Online)
Year 2002
Volume 8
Pages 173-83
Authors Iribarne F, Paulino M, Aguilera S, Murphy M, Tapia O
Title Docking and molecular dynamics studies at trypanothione reductase and glutathione reductase active sites.
Related PDB
Related UniProtKB
[53]
Resource
Comments
Medline ID
PubMed ID 12729762
Journal J Mol Biol
Year 2003
Volume 328
Pages 893-907
Authors Sarma GN, Savvides SN, Becker K, Schirmer M, Schirmer RH, Karplus PA
Title Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development.
Related PDB 1onf
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 16493712
Journal Angew Chem Int Ed Engl
Year 2006
Volume 45
Pages 1881-6
Authors Urig S, Fritz-Wolf K, R?au R, Herold-Mende C, T?th K, Davioud-Charvet E, Becker K
Title Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases.
Related PDB 2aaq
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 16910673
Journal J Am Chem Soc
Year 2006
Volume 128
Pages 10784-94
Authors Bauer H, Fritz-Wolf K, Winzer A, K?hner S, Little S, Yardley V, Vezin H, Palfey B, Schirmer RH, Davioud-Charvet E
Title A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme.
Related PDB 2gh5
Related UniProtKB
[56]
Resource
Comments
Medline ID
PubMed ID 17554778
Journal Proteins
Year 2007
Volume 68
Pages 972-9
Authors Yu J, Zhou CZ
Title Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae.
Related PDB 2hqm
Related UniProtKB

Comments
This enzyme was transferred from E.C. 1.6.4.2 to E.C. 1.8.1.7.
This enzyme catalyzes the following reactions (see [3], [13], [16]):
(A) Hydride or electron transfer from NADPH to FAD, forming FADH2 (Reduction of FAD by NADPH):
(A0) This hydride transfer involves Glu201, Lys 66 and Tyr197.
(B) Electron transfer from FADH2 to redox-active disulfide bond Cys63-Cys58 (oxidized form), forming reduced form of cysteine residues:
(B1) The C4a atom of flavin (FADH2) makes a nucleophilic attack on the sulfur atom of Cys63, causing Cys58 to leave as a thiolate ion (SN2-like reaction).
(B2) This reaction proceeds via a short-lived (unstable) intermediate (covalent bond between C4a of flavin and sulfur atom of Cys63).
(B3) The fate of the transferred hydrogen on the flavin is not clear (see [16]).
(C) Electron transfer from Cys58 (and Cys63) to glutathione disulfide (or oxidized glutathione, GSSG), producing two glutathione molecules (GSH) (see [3], [16]):
(C0) Glu472 modulates the pKa of His467'. Moreover, Tyr114 might assist His467' (see [40]).
(C1) His467' acts as a general base to deprotonate the sulfur of Cys58.
(C2) Cys58 makes a nucleophilic attack on the Cys-I of GSSG, forming a mixed disulfide bond between C58 and GSH-I, and causing Cys-II to leave as a thiolate ion. (During this reaction, electrons shift from Cys58 to Cys-I.)
(C2') The protonated sidechain of His467' polarizes the mixed disulfide bond.
(C3) Cys63 makes a nucleophilic attack on the Cys58, forming a disulfide bond again, and causing Cys-I to leave as a thiolate ion. Here, His467' acts as a general acid to protonate the thiolate of Cys-I.

Created Updated
2004-12-22 2009-02-26