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) |
|---|---|
| 3.30.390.30 : Enolase-like; domain 1 | M00163 T00017 T00233 T00242 |
| 3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00042 D00045 D00064 D00071 T00004 T00015 T00017 T00025 T00211 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. |
|---|---|---|
| MAP00251 | Glutamate metabolism | |
| MAP00480 | Glutathione 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 16238 |
17858 17858 |
16474 16474 |
15378 15378 |
16856 16856 |
18009 18009 |
||||||
| PubChem |
643975 643975 |
11215652 65359 11215652 65359 |
5884 5884 |
1038 1038 |
124886 25246407 124886 25246407 |
5886 5886 |
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| 1gerA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gerB01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesB01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1getA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1getB01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1geuA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1geuB01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hqmA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hqmB01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1onfA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bwcA01 |
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Bound:FAD | Unbound | Unbound | Analogue:AJ3 | Unbound | Unbound | |
| 1dncA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:GTT-CYS_58 | |
| 1graA01 |
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Bound:FAD | Bound:GSH-GSH | Unbound | Unbound | Unbound | Unbound | |
| 1grbA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1greA01 |
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Bound:FAD | Unbound | Unbound | Bound:GSH_482 | Unbound | Intermediate-bound:GSH_481-CYS_58 | |
| 1grfA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:ACM-CYS_58 | |
| 1grgA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CEC-CYS_58 | |
| 1grtA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gsnA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:GTT-CYS_58 | |
| 1xanA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2aaqA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2gh5A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:ELI-CYS_58 | |
| 2gh5B01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:ELI-CYS_58 | |
| 2grtA01 |
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Bound:FAD | Bound:GDS | Unbound | Unbound | Unbound | Unbound | |
| 3grsA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3grtA01 |
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Bound:FAD | Analogue:TS2 | Unbound | Unbound | Unbound | Unbound | |
| 4gr1A01 |
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Bound:FAD | Analogue:RGS | Unbound | Unbound | Unbound | Unbound | |
| 4grtA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GCG-CYS_58 | |
| 5grtA01 |
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Bound:FAD | Analogue:TS4 | Unbound | Unbound | Unbound | Unbound | |
| 1gerA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gerB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1getA02 |
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Unbound | Unbound | Unbound | Unbound | Bound:NAP | Unbound | |
| 1getB02 |
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Unbound | Unbound | Unbound | Unbound | Bound:NAP | Unbound | |
| 1geuA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:NAD | Unbound | |
| 1geuB02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:NAD | Unbound | |
| 2hqmA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hqmB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1onfA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bwcA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1dncA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1graA02 |
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Unbound | Unbound | Analogue:NDP | Unbound | Unbound | Unbound | |
| 1grbA02 |
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Unbound | Unbound | Bound:NDP | Unbound | Analogue:NAD | Unbound | |
| 1greA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grfA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grgA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grtA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gsnA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xanA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2aaqA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2gh5A02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2gh5B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2grtA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3grsA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3grtA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4gr1A02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4grtA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 5grtA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gerA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gerB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gesB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1getA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1getB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1geuA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1geuB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hqmA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2hqmB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1onfA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bwcA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1dncA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1graA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grbA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1greA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grfA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grgA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1grtA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1gsnA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xanA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2aaqA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2gh5A03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2gh5B03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 2grtA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3grsA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3grtA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4gr1A03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 4grtA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 5grtA03 |
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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 |
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CYS 42;CYS 47;LYS 50 | disulfide bonded/oxidized form C42-C47 | |||
| 1gerB01 |
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CYS 42;CYS 47;LYS 50 | disulfide bonded/oxidized form C42-C47 | |||
| 1gesA01 |
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CYS 42;CYS 47;LYS 50 | disulfide bonded/oxidized form C42-C47 | |||
| 1gesB01 |
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CYS 42;CYS 47;LYS 50 | disulfide bonded/oxidized form C42-C47 | |||
| 1getA01 |
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CYS 42;CYS 47;LYS 50 | reduced form C42, C47 | |||
| 1getB01 |
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CYS 42;CYS 47;LYS 50 | reduced form C42, C47 | |||
| 1geuA01 |
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CYS 42;CYS 47;LYS 50 | reduced form C42, C47 | |||
| 1geuB01 |
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CYS 42;CYS 47;LYS 50 | reduced form C42, C47 | |||
| 2hqmA01 |
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CYS 61;CYS 66;LYS 69 | disulfide bonded/oxidized form C61-C66 | |||
| 2hqmB01 |
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CYS 61;CYS 66;LYS 69 | disulfide bonded/oxidized form C61-C66 | |||
| 1onfA01 |
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CYS 39;CYS 44;LYS 47 | reduced form C39, C44 | |||
| 1bwcA01 |
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CYS 58;CYS 63;LYS 66 | disulfide bonded/oxidized form C58-C63 | |||
| 1dncA01 |
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CYS 58; ;LYS 66 | CSD 63(sulfinylated) | modified C63 | ||
| 1graA01 |
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CYS 58;CYS 63;LYS 66 | disulfide bonded/oxidized form C58-C63 | |||
| 1grbA01 |
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CYS 58;CYS 63;LYS 66 | reduced form C58, C63 | |||
| 1greA01 |
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CYS 58;CYS 63;LYS 66 | ||||
| 1grfA01 |
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CYS 58;CYS 63;LYS 66 | ||||
| 1grgA01 |
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CYS 58;CYS 63;LYS 66 | ||||
| 1grtA01 |
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CYS 58;CYS 63;LYS 66 | mutant A34E, R37W, disulfide bonded/oxidized form C58-C63 | |||
| 1gsnA01 |
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CYS 58; ;LYS 66 | CSO 63(sulfenylated) | |||
| 1xanA01 |
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CYS 58;CYS 63;LYS 66 | disulfide bonded/oxidized form C58-C63 | |||
| 2aaqA01 |
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CYS 58;CYS 63;LYS 66 | reduced form C58, C63 | |||
| 2gh5A01 |
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CYS 58;CYS 63;LYS 66 | ||||
| 2gh5B01 |
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CYS 58;CYS 63;LYS 66 | ||||
| 2grtA01 |
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CYS 58;CYS 63;LYS 66 | mutant A34E, R37W, disulfide bonded/oxidized form C58-C63 | |||
| 3grsA01 |
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CYS 58;CYS 63;LYS 66 | disulfide bonded/oxidized form C58-C63 | |||
| 3grtA01 |
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CYS 58;CYS 63;LYS 66 | mutant A34E, R37W, disulfide bonded/oxidized form C58-C63 | |||
| 4gr1A01 |
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CYS 58;CYS 63;LYS 66 | disulfide bonded/oxidized form C58-C63 | |||
| 4grtA01 |
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CYS 58;CYS 63;LYS 66 | mutant A34E, R37W | |||
| 5grtA01 |
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CYS 58;CYS 63;LYS 66 | mutant A34E, R37W, disulfide bonded/oxidized form C58-C63 | |||
| 1gerA02 |
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TYR 177;GLU 181 | ||||
| 1gerB02 |
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TYR 177;GLU 181 | ||||
| 1gesA02 |
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TYR 177;GLU 181 | mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P | |||
| 1gesB02 |
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TYR 177;GLU 181 | mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P | |||
| 1getA02 |
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TYR 177;GLU 181 | ||||
| 1getB02 |
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TYR 177;GLU 181 | ||||
| 1geuA02 |
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TYR 177;GLU 181 | mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P | |||
| 1geuB02 |
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TYR 177;GLU 181 | mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P | |||
| 2hqmA02 |
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TYR 207;GLU 211 | ||||
| 2hqmB02 |
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TYR 207;GLU 211 | ||||
| 1onfA02 |
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TYR 185;GLU 189 | ||||
| 1bwcA02 |
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TYR 197;GLU 201 | ||||
| 1dncA02 |
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TYR 197;GLU 201 | ||||
| 1graA02 |
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TYR 197;GLU 201 | ||||
| 1grbA02 |
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TYR 197;GLU 201 | ||||
| 1greA02 |
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TYR 197;GLU 201 | ||||
| 1grfA02 |
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TYR 197;GLU 201 | ||||
| 1grgA02 |
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TYR 197;GLU 201 | ||||
| 1grtA02 |
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TYR 197;GLU 201 | ||||
| 1gsnA02 |
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|
|
TYR 197;GLU 201 | CSO 234(sulfenylated);CSO 284(sulfenylated) | |||
| 1xanA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 2aaqA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 2gh5A02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 2gh5B02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 2grtA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 3grsA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 3grtA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 4gr1A02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 4grtA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 5grtA02 |
|
|
|
|
|
TYR 197;GLU 201 | ||||
| 1gerA03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1gerB03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1gesA03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1gesB03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1getA03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1getB03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1geuA03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 1geuB03 |
|
|
|
|
|
HIS 439;GLU 444 | ||||
| 2hqmA03 |
|
|
|
|
|
HIS 472;GLU 477 | ||||
| 2hqmB03 |
|
|
|
|
|
HIS 472;GLU 477 | ||||
| 1onfA03 |
|
|
|
|
|
HIS 484;GLU 489 | ||||
| 1bwcA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1dncA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1graA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1grbA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1greA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1grfA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1grgA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1grtA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 1gsnA03 |
|
|
|
|
|
HIS 467;GLU 472 | CSO 423(sulfenylated) | |||
| 1xanA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 2aaqA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 2gh5A03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 2gh5B03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 2grtA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 3grsA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 3grtA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 4gr1A03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 4grtA03 |
|
|
|
|
|
HIS 467;GLU 472 | ||||
| 5grtA03 |
|
|
|
|
|
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 |
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| 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. |
| 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. |
| 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, |
| 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, |
| 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. |
| 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, |
| 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. |
| 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. |
| 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, |
| 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, |
| 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, |
| 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. |
| 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, |
| 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. |
| 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. This enzyme catalyzes the following reactions (see [3], (A) Hydride or electron transfer from NADPH to FAD, (A0) This hydride transfer involves Glu201, (B) Electron transfer from FADH2 to redox-active disulfide bond Cys63-Cys58 (oxidized form), (B1) The C4a atom of flavin (FADH2) makes a nucleophilic attack on the sulfur atom of Cys63, (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, (C0) Glu472 modulates the pKa of His467'. (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, (C2') The protonated sidechain of His467' polarizes the mixed disulfide bond. (C3) Cys63 makes a nucleophilic attack on the Cys58, |
| Created | Updated |
|---|---|
| 2004-12-22 | 2009-02-26 |