Katoh M, Hiratake J, Oda J
Institute for Chemical Research, Kyoto University, Japan.
Biosci Biotechnol Biochem. 1998 Jul;62(7):1455-7. doi: 10.1271/bbb.62.1455.
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.
