Literature summary for 1.8.1.7 extracted from

Rousar, T.; Parik, P.; Kucera, O.; Bartos, M.; Cervinkova, Z.
Glutathione reductase is inhibited by acetaminophen-glutathione conjugate in vitro (2010), Physiol. Res., 59, 225-232.

Search for more literature for 1.8.1.7

Inhibitors

Inhibitors	Comment	Organism	Structure
acetaminophen-glutathione conjugate	the enzyme activity is inhibited to 48.1% after treatment with 2.96 mM acetaminophen-glutathione conjugate, the enzyme activity (from hepatocytes lysate) is decreased to 79%, 67%, and 397%, in 0.37, 1.48 and 3.7 mM concentration of the conjugate, respectively, at pH 7.6 at 25°C	Rattus norvegicus
acetaminophen-glutathione conjugate	the enzyme activity is inhibited to 52.7% after treatment with 2.96 mM acetaminophen-glutathione conjugate, at pH 7.6 at 25°C	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-
Saccharomyces cerevisiae	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Rattus norvegicus	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
glutathione reductase	-	Rattus norvegicus
glutathione reductase	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Rattus norvegicus
FAD	-	Saccharomyces cerevisiae
NADPH	-	Rattus norvegicus
NADPH	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)