gamma-glutamylcysteine synthetase

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γ-glu·ta·myl·cys·teine syn·the·tase

an enzyme that catalyzes the first step in glutathione biosynthesis, reacting l-glutamate, l-cysteine, and ATP to form γ-glutamylcysteine, ADP, and orthophosphate; inhibited by thiols such as glutathione and cysteamine.
References in periodicals archive ?
Mulcahy, "Regulation of gamma-glutamylcysteine synthetase subunit gene expression: insights into transcriptional control of antioxidant defenses," Free Radical Research, vol.
Gipp, "Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene," Biochemical and Biophysical Research Communications, vol.
We have clear evidence that HGF can stimulate the GSH system machinery, particularly the key enzyme in GSH synthesis, the gamma-glutamylcysteine synthetase ([gamma]-GCS), which, in addition, increases GSH content [5, 17]; in the present study we did find the same effect in Chow cells; interestingly, [gamma]-GCS content in HC cells slightly decreased with HGF treatment, but GSH/GSSG ratio presented a different behavior; HGF induced a decrease in the tripeptide ratio at 6 h comparing with Chow cells, and at 12 h GSH ratio exhibited a significant recovery.
Crystal structure of gamma-glutamylcysteine synthetase: insights in to the mechanism of catalysis by a key enzyme for glutathione homeostasis.
Cadmium-mediated oxidative stress in alveolar epithelial cells induces the expression of gamma-glutamylcysteine synthetase catalytic subunit and glutathione S-transferase alpha and pi isoforms: potential role of activator protein-1.
Sulforaphane also induces expression of gamma-glutamylcysteine synthetase light subunit but not the heavy subunit, and this induction is associated with moderate increases in intracellular glutathione levels.
Knock down of gamma-glutamylcysteine synthetase in rat causes a cetaminophen-induced hepatotoxicity.
Resistance of Leishmania donovani to sodium stibogluconate is related to the expression of host and parasite gamma-glutamylcysteine synthetase. Antimicrob Agents Chemother 2006; 50 : 88-95.
Mulcahy, "Up-regulation of the human gamma-glutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element," Biochemical and Biophysical Research Communications, vol.
Cancer cells produce an enzyme called gamma-glutamylcysteine synthetase (GCS), which metabolizes and inactivates cyclophosphamide.
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