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Literature summary extracted from
- The inhibition kinetics of yeast glutathione reductase by some metal ions (2007), J. Enzyme Inhib. Med. Chem., 22, 489-495.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | Ca2+ | inhibition is non-competitive with respect to GSSG and uncompetitive with respect to NADPH | Saccharomyces cerevisiae |  |
| 1.8.1.7 | Cd2+ | - |
Saccharomyces cerevisiae | |
| 1.8.1.7 | Ni2+ | inhibition is competitive with respect to GSSG and uncompetitive with respect to NADPH | Saccharomyces cerevisiae | |
| 1.8.1.7 | Zn2+ | glutathione reductase is non-competitively inhibited up to 2 mM and activated above this concentration | Saccharomyces cerevisiae | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | Zn2+ | glutathione reductase is non-competitively inhibited up to 2 mM and activated above this concentration | Saccharomyces cerevisiae | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.7 | Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.7 | GSSG + NADPH + H+ | - |
Saccharomyces cerevisiae | glutathione + NADP+ | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | NADPH | - |
Saccharomyces cerevisiae | |
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Release 2023.1 (January 2023)
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