gamma-Glutamylcysteine synthetase is inactivated by incubation with low concentrations of L-2-amino-4-oxo-5-chloropentanoate. Very low concentrations of magnesium ions or certain other divalent cations are required for inactivation. L-Glutamate, but not D-glutamate or L-glutamine, protected against inactivation and the protective effect of L-glutamate was increased in the presence of ATP or ADP. L-alpha-Aminobutyrate increased the rate of inactivation by the chloroketone. When the chloroketone was added to the dipeptide synthesis system, inhibition was competitive with L-glutamate. Iodoacetamide also inhibited the enzyme; however, this reagent is much less effective than the chloroketone and inhibition by iodoacetamide is less effectively prevented by L-glutamate. Studies with 14C-labeled chloroketone showed that this reagent binds stoichiometrically to the enzyme, and that it binds exclusively to its heavy subunit.
Covalent interaction of L-2-amino-4-oxo-5-chloropentanoate at glutamate binding site of gamma-glutamylcysteine synthetase.
Published 1977 in Journal of Biological Chemistry
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- Publication year
1977
- Venue
Journal of Biological Chemistry
- Publication date
1977-04-25
- Fields of study
Medicine, Chemistry
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Semantic Scholar, PubMed
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