Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.

@article{Christensen1990BetalactamasesAF,
  title={Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.},
  author={Henriette Christensen and Marie Th{\'e}r{\`e}se Martin and S. G. Waley},
  journal={The Biochemical journal},
  year={1990},
  volume={266 3},
  pages={853-61}
}
The rate constants for both acylation and deacylation of beta-lactamase PC1 from Staphylococcus aureus and the RTEM beta-lactamase from Escherichia coli were determined by the acid-quench method [Martin & Waley (1988) Biochem. J. 254, 923-925] with several good substrates, and, for a wider range of substrates, of beta-lactamase I from Bacillus cereus. The values of the acylation and deacylation rate constants for benzylpenicillin were approximately the same (i.e. differing by no more than 2… CONTINUE READING

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