Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1

@article{Fernea2016KineticsOT,
  title={Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1},
  author={Adriana Fernea and M. Galleni and J. Fr{\`e}re},
  journal={Antimicrobial Agents and Chemotherapy},
  year={2016},
  volume={60},
  pages={1747 - 1750}
}
ABSTRACT The chromosome-encoded class C β-lactamase CHE-1 produced by Enterobacter cloacae exhibits a lower sensitivity to avibactam than the P99 enzyme from which it is derived by a 6-residue deletion in the H-10 helix. In the present study, we investigated the sensitivity of CHE-1 to two other β-lactamase inhibitors: LK-157 (or Lek 157), a tricyclic β-lactam, and BAL29880, a bridged monobactam. With both compounds, the second-order rate constants for inactivation were significantly lower for… Expand

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