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Literature summary extracted from

  • Murakami, K.; Tsubouchi, R.; Fukayama, M.; Yoshino, M.
    Copper-dependent inhibition and oxidative inactivation with affinity cleavage of yeast glutathione reductase (2014), Biometals, 27, 551-558 .
    View publication on PubMed

Inhibitors

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

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 glutathione disulfide + NADPH + H+
-
 Saccharomyces cerevisiae 2 glutathione + NADP+
-
 ?

Ki Value [mM]

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