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Literature summary for 1.8.1.7 extracted from
- 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)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant in Escherichia coli, structure modeling | Anabaena sp. |
Protein Variants
| 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 [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km of wild-type and mutants | Anabaena sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Anabaena sp. | - |
PCC 7120, cyanobacterium | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type and recombinant from Escherichia coli | Anabaena sp. |
Reaction
| 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 and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GSSG + NADPH | - |
Anabaena sp. | glutathione + NADP+ | - |
ir |  |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Anabaena sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
NADPH + GSSG | Anabaena sp. |
| 8 | - |
NADH + GSSG | Anabaena sp. |
Cofactor
| 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. | |
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Release 2023.1 (January 2023)
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