PMID:9720231
| Citation |
Katoh, M, Hiratake, J and Oda, J (1998) ATP-dependent inactivation of Escherichia coli gamma-glutamylcysteine synthetase by L-glutamic acid gamma-monohydroxamate. Biosci. Biotechnol. Biochem. 62:1455-7 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Adenosine Triphosphate/pharmacology; Aspartate Aminotransferases/antagonists & inhibitors; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Glutamate-Cysteine Ligase/antagonists & inhibitors; Glutamates/pharmacology; Hydroxamic Acids/pharmacology; Phosphorylation |
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