Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant in Escherichia coli, structure modeling | Anabaena sp. |
Protein Variants | Comment | Organism |
---|---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km of wild-type and mutants | Anabaena sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Anabaena sp. | - |
PCC 7120, cyanobacterium | - |
Purification (Comment) | Organism |
---|---|
wild-type and recombinant from Escherichia coli | Anabaena sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ | member of pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes | Anabaena sp. | |
2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ | substrate and cofactor binding site, three-dimensional structure | Anabaena sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GSSG + NADPH | - |
Anabaena sp. | glutathione + NADP+ | - |
ir |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Anabaena sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
NADPH + GSSG | Anabaena sp. |
8 | - |
NADH + GSSG | Anabaena sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD enzyme | Anabaena sp. | |
NADH | 48fold less activity than with NADPH | Anabaena sp. | |
NADPH | 48fold more activity than with NADH | Anabaena sp. |