Literature summary extracted from
Danielson, U.H.; Jiang, F.; Hansson, L.O.; Mannervik, B.
Probing the kinetic mechanism and coenzyme specificity of glutathione reductase from the Cyanobacterium Anabaena PCC 7120 by redesign of the pyridine-nucleotide-binding site (1999), Biochemistry, 38, 9254-9263.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.8.1.7 |
expression of wild-type and mutant in Escherichia coli, structure modeling |
Anabaena sp. |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.8.1.7 |
additional information |
a mutant lacking a loop involved in ligand binding, showing reduced activity, and a mutant with a modified loop, which is more efficient with NADPH and NADH |
Anabaena sp. |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
1.8.1.7 |
additional information |
- |
additional information |
Km of wild-type and mutants |
Anabaena sp. |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.8.1.7 |
Anabaena sp. |
- |
PCC 7120, cyanobacterium |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.8.1.7 |
wild-type and recombinant from Escherichia coli |
Anabaena sp. |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.8.1.7 |
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ |
member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes |
Anabaena sp. |
|
1.8.1.7 |
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ |
substrate and cofactor binding site, three-dimensional structure |
Anabaena sp. |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.8.1.7 |
GSSG + NADPH |
- |
Anabaena sp. |
glutathione + NADP+ |
- |
ir |
|
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.8.1.7 |
30 |
- |
assay at |
Anabaena sp. |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.8.1.7 |
7 |
- |
NADPH + GSSG |
Anabaena sp. |
1.8.1.7 |
8 |
- |
NADH + GSSG |
Anabaena sp. |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.8.1.7 |
FAD |
FAD enzyme |
Anabaena sp. |
|
1.8.1.7 |
NADH |
48fold less activity than with NADPH |
Anabaena sp. |
|
1.8.1.7 |
NADPH |
48fold more activity than with NADH |
Anabaena sp. |
|