EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.8.1.7 | Cu+ | presence of Cu+ inhibits noncompetitively with respect to the substrate GSSG and NADPH and inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase | Saccharomyces cerevisiae | |
1.8.1.7 | Cu2+ | presence of Cu2+ inhibits noncompetitively with respect to the substrate GSSG and NADPH and inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase. Copper binds to sites apart from the substrate sites, causing the peptide cleavage by hydroxyl radical | Saccharomyces cerevisiae | |
1.8.1.7 | H2O2 | inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.1.7 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.7 | glutathione disulfide + NADPH + H+ | - |
Saccharomyces cerevisiae | 2 glutathione + NADP+ | - |
? |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.1.7 | 0.00035 | - |
Cu+ | pH 7.8, 37°C | Saccharomyces cerevisiae | |
1.8.1.7 | 0.001 | - |
Cu2+ | pH 7.8, 37°C | Saccharomyces cerevisiae |