Literature summary for 1.8.1.7 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 .

Search for more literature for 1.8.1.7

Inhibitors

Inhibitors	Comment	Organism	Structure
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
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
H2O2	inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
glutathione disulfide + NADPH + H+	-	Saccharomyces cerevisiae	2 glutathione + NADP+	-	?

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00035	-	Cu+	pH 7.8, 37°C	Saccharomyces cerevisiae
0.001	-	Cu2+	pH 7.8, 37°C	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)