ATP-dependent inactivation of Escherichia coli gamma-glutamylcysteine synthetase by L-glutamic acid gamma-monohydroxamate.
Incubation of Escherichia coli gamma-glutamylcysteine synthetase with L-glutamic acid gamma-monohydroxamate and ATP caused slow but irreversible inhibition of the enzyme, and more than 90% activity was lost in three days. The enzyme was not inactivated when ATP was absent or L-aspartic acid beta-monohydroxamate was substituted for L-glutamic acid gamma-monohydroxamate, suggesting that the inactivation process reflected a mechanism-based reaction of L-glutamic acid gamma-monohydroxamate and ATP.
Katoh
M
M
Institute for Chemical Research, Kyoto University, Japan.
Hiratake
J
J
Oda
J
J
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D001219:Aspartate Aminotransferases / Q000037:antagonists & inhibitors; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology*; D005721:Glutamate-Cysteine Ligase / Q000037:antagonists & inhibitors*; D005971:Glutamates / Q000494:pharmacology*; D006877:Hydroxamic Acids / Q000494:pharmacology*; D010766:Phosphorylation
D004791:Enzyme Inhibitors; D005971:Glutamates; D006877:Hydroxamic Acids; C050614:glutamate-gamma-hydroxamic acid; D000255:Adenosine Triphosphate; D001219:Aspartate Aminotransferases; D005721:Glutamate-Cysteine Ligase