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Literature summary 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.
    View publication on PubMed

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.7 NADPH
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.8.1.7 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