Literature summary for 1.8.1.7 extracted from

Kedrowski, B.L.; Gutow, J.H.; Stock, G.; Smith, M.; Jordan, C.; Masterson, D.S.
Glutathione reductase activity with an oxidized methylated glutathione analog (2014), J. Enzyme Inhib. Med. Chem., 29, 491-494.

Search for more literature for 1.8.1.7

Inhibitors

Inhibitors	Comment	Organism	Structure
L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide	competitive inhibitor	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
glutathione disulfide + NADPH + H+	Saccharomyces cerevisiae	-	glutathione + NADP+	-	ir
additional information	Saccharomyces cerevisiae	no activity with L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide	?	-	?

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	glutathione + NADP+	-	ir
additional information	no activity with L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide	Saccharomyces cerevisiae	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.01464	-	L-gamma-glutamyl-2-methyl-L-cysteinyl-glycine disulfide	in 100mM in potassium phosphate, pH 7.5, temperature not specified in the publication	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)