|
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 |
KEGG pathways | MAP code | Pathways |
---|
MAP00251 | Glutamate metabolism | MAP00480 | Glutathione metabolism |
UniProtKB:Accession Number | P06715 | P41921 | Q94655 | P00390 |
---|
Entry name | GSHR_ECOLI | GSHR_YEAST | GSHR_PLAFK | GSHR_HUMAN |
---|
Activity | 2 glutathione + NADP(+) = glutathione disulfide + NADPH. | 2 glutathione + NADP(+) = glutathione disulfide + NADPH. | 2 glutathione + NADP(+) = glutathione disulfide + NADPH. | 2 glutathione + NADP(+) = glutathione disulfide + NADPH. |
---|
Subunit | Homodimer. |
| Homodimer. | Homodimer, disulfide-linked. |
---|
Subcellular location | Cytoplasm. | Cytoplasm (By similarity). | Cytoplasm. | Mitochondrion. Cytoplasm. |
---|
Cofactor | Binds 1 FAD per subunit. | Binds 1 FAD per subunit (By similarity). | Binds 1 FAD per subunit (By similarity). | Binds 1 FAD per subunit. |
---|
Compound table: links to PDB-related databases & PoSSuM |
---|
| Cofactors | Substrates | Products | intermediates |
---|
KEGG-id | C00016 | C00127 | C00005 | C00080 | C00051 | C00006 |
|
---|
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
| 11215652 65359
| 5884
| 1038
| 124886 25246407
| 5886
|
|
---|
| | | | | | | | | | | | | | |
---|
1gerA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gerB01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesB01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1getA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1getB01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1geuA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1geuB01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2hqmA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2hqmB01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1onfA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1bwcA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Analogue:AJ3 | Unbound | Unbound |
---|
1dncA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-bound:GTT-CYS 58 |
---|
1graA01 |  |  |  |  |  |  |  | Bound:FAD | Bound:GSH-GSH | Unbound | | Unbound | Unbound | Unbound |
---|
1grbA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1greA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Bound:GSH 482 | Unbound | Intermediate-bound:GSH 481-CYS 58 |
---|
1grfA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-analogue:ACM-CYS 58 |
---|
1grgA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-analogue:CEC-CYS 58 |
---|
1grtA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gsnA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-bound:GTT-CYS 58 |
---|
1xanA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2aaqA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2gh5A01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-analogue:ELI-CYS 58 |
---|
2gh5B01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-analogue:ELI-CYS 58 |
---|
2grtA01 |  |  |  |  |  |  |  | Bound:FAD | Bound:GDS | Unbound | | Unbound | Unbound | Unbound |
---|
3grsA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
3grtA01 |  |  |  |  |  |  |  | Bound:FAD | Analogue:TS2 | Unbound | | Unbound | Unbound | Unbound |
---|
4gr1A01 |  |  |  |  |  |  |  | Bound:FAD | Analogue:RGS | Unbound | | Unbound | Unbound | Unbound |
---|
4grtA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound | Intermediate-analogue:GCG-CYS 58 |
---|
5grtA01 |  |  |  |  |  |  |  | Bound:FAD | Analogue:TS4 | Unbound | | Unbound | Unbound | Unbound |
---|
1gerA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gerB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1getA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Bound:NAP | Unbound |
---|
1getB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Bound:NAP | Unbound |
---|
1geuA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Analogue:NAD | Unbound |
---|
1geuB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Analogue:NAD | Unbound |
---|
2hqmA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2hqmB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1onfA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1bwcA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1dncA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1graA02 |  |  |  |  |  |  |  | Unbound | Unbound | Analogue:NDP | | Unbound | Unbound | Unbound |
---|
1grbA02 |  |  |  |  |  |  |  | Unbound | Unbound | Bound:NDP | | Unbound | Analogue:NAD | Unbound |
---|
1greA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grfA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grgA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grtA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gsnA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1xanA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2aaqA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2gh5A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2gh5B02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2grtA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
3grsA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
3grtA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
4gr1A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
4grtA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
5grtA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gerA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gerB03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gesB03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1getA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1getB03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1geuA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1geuB03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2hqmA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2hqmB03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1onfA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1bwcA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1dncA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1graA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grbA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1greA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grfA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grgA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1grtA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1gsnA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
1xanA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2aaqA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2gh5A03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2gh5B03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
2grtA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
3grsA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
3grtA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
4gr1A03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
4grtA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
5grtA03 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound | Unbound |
---|
Active-site residues | resource |
---|
PDB;2grt & Swiss-prot;P06715, P00390 & literature [7], [9], [16], [39], [46] | pdb | Catalytic residues | Modified residues | comment |
---|
| | | | | | | | | | |
---|
1gerA01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| disulfide bonded/oxidized form C42-C47
|
---|
1gerB01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| disulfide bonded/oxidized form C42-C47
|
---|
1gesA01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| disulfide bonded/oxidized form C42-C47
|
---|
1gesB01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| disulfide bonded/oxidized form C42-C47
|
---|
1getA01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| reduced form C42, C47
|
---|
1getB01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| reduced form C42, C47
|
---|
1geuA01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| reduced form C42, C47
|
---|
1geuB01 |  |  |  |  |  |  |  | CYS 42;CYS 47;LYS 50
|
| reduced form C42, C47
|
---|
2hqmA01 |  |  |  |  |  |  |  | CYS 61;CYS 66;LYS 69
|
| disulfide bonded/oxidized form C61-C66
|
---|
2hqmB01 |  |  |  |  |  |  |  | CYS 61;CYS 66;LYS 69
|
| disulfide bonded/oxidized form C61-C66
|
---|
1onfA01 |  |  |  |  |  |  |  | CYS 39;CYS 44;LYS 47
|
| reduced form C39, C44
|
---|
1bwcA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| disulfide bonded/oxidized form C58-C63
|
---|
1dncA01 |  |  |  |  |  |  |  | CYS 58; ;LYS 66
| CSD 63(sulfinylated)
| modified C63
|
---|
1graA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| disulfide bonded/oxidized form C58-C63
|
---|
1grbA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| reduced form C58, C63
|
---|
1greA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
|
|
---|
1grfA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
|
|
---|
1grgA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
|
|
---|
1grtA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
|
---|
1gsnA01 |  |  |  |  |  |  |  | CYS 58; ;LYS 66
| CSO 63(sulfenylated)
|
|
---|
1xanA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| disulfide bonded/oxidized form C58-C63
|
---|
2aaqA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| reduced form C58, C63
|
---|
2gh5A01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
|
|
---|
2gh5B01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
|
|
---|
2grtA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
|
---|
3grsA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| disulfide bonded/oxidized form C58-C63
|
---|
3grtA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
|
---|
4gr1A01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| disulfide bonded/oxidized form C58-C63
|
---|
4grtA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| mutant A34E, R37W
|
---|
5grtA01 |  |  |  |  |  |  |  | CYS 58;CYS 63;LYS 66
|
| mutant A34E, R37W, disulfide bonded/oxidized form C58-C63
|
---|
1gerA02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
|
|
---|
1gerB02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
|
|
---|
1gesA02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
| mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
|
---|
1gesB02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
| mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
|
---|
1getA02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
|
|
---|
1getB02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
|
|
---|
1geuA02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
| mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
|
---|
1geuB02 |  |  |  |  |  |  |  | TYR 177;GLU 181
|
| mutant A179G, A183G, V197E, R198M, K199F, H200D, R204P
|
---|
2hqmA02 |  |  |  |  |  |  |  | TYR 207;GLU 211
|
|
|
---|
2hqmB02 |  |  |  |  |  |  |  | TYR 207;GLU 211
|
|
|
---|
1onfA02 |  |  |  |  |  |  |  | TYR 185;GLU 189
|
|
|
---|
1bwcA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1dncA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1graA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1grbA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1greA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1grfA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1grgA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1grtA02 |  |  |  |  |  |  |  | TYR 197;GLU 201
|
|
|
---|
1gsnA02 |  |  |  |  |  |  |  | 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] |
---|
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 UniProtKB | P00390 |
---|
[2] |
---|
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. |
---|
[3] |
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PubMed ID | 6822532 |
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Journal | J Biol Chem |
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Year | 1983 |
---|
Volume | 258 |
---|
Pages | 1752-7 |
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Authors | Pai EF, Schulz GE |
---|
Title | The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. |
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[4] |
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PubMed ID | 6697994 |
---|
Journal | Eur J Biochem |
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Year | 1984 |
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Volume | 138 |
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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. |
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[5] |
---|
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. |
---|
[6] |
---|
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. |
---|
[7] |
---|
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. |
---|
[8] |
---|
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. |
---|
[9] |
---|
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] |
---|
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. |
---|
[11] |
---|
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. |
---|
[12] |
---|
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. |
---|
[13] |
---|
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. |
---|
[14] |
---|
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. |
---|
[15] |
---|
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. |
---|
[16] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[17] |
---|
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. |
---|
[18] |
---|
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. |
---|
[19] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[20] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[21] |
---|
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. |
---|
[22] |
---|
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. |
---|
[23] |
---|
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. |
---|
[24] |
---|
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. |
---|
[25] |
---|
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 UniProtKB | P06715 |
---|
[26] |
---|
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. |
---|
[27] |
---|
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. |
---|
[28] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[29] |
---|
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] |
---|
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. |
---|
[31] |
---|
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. |
---|
[32] |
---|
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. |
---|
[33] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[34] |
---|
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. |
---|
[35] |
---|
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 UniProtKB | Q94655 |
---|
[36] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[37] |
---|
Comments | NMR structure |
---|
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 |
---|
[38] |
---|
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. |
---|
[39] |
---|
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. |
---|
[40] |
---|
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. |
---|
[41] |
---|
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. |
---|
[42] |
---|
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. |
---|
[43] |
---|
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. |
---|
[44] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[45] |
---|
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. |
---|
[46] |
---|
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. |
---|
[47] |
---|
Comments | X-ray crystallography |
---|
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 |
---|
[48] |
---|
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. |
---|
[49] |
---|
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. |
---|
[50] |
---|
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. |
---|
[51] |
---|
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. |
---|
[52] |
---|
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. |
---|
[53] |
---|
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 |
---|
[54] |
---|
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 |
---|
[55] |
---|
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 |
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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. |
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Related PDB | 2gh5 |
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[56] |
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PubMed ID | 17554778 |
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Journal | Proteins |
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Year | 2007 |
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Volume | 68 |
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Pages | 972-9 |
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Authors | Yu J, Zhou CZ |
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Title | Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae. |
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Related PDB | 2hqm |
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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.
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created | updated |
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2004-12-22 | 2009-02-26 |
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