Kinetic studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid.

@article{Fisher1978KineticSO,
  title={Kinetic studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid.},
  author={Julie Fisher and Rebecca Charnas and Jeremy Knowles},
  journal={Biochemistry},
  year={1978},
  volume={17 11},
  pages={2180-4}
}
The kinetic details of the irreversible inactivation of the Escherichia coli RTEM beta-lactamase by clavulanic acid have been elucidated. Clavulanate is destroyed by the enzyme and simultaneously inhibits it by producing two catalytically inactive forms. One of these is transiently stable and decomposes to free enzyme (k = 3.8 X 10(-3) S-1), while the other corresponds to an irreversibly inactivated form. The transient complex is formed from the Michaelis complex at a rate (k approximately 3 X… CONTINUE READING

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