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

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 CHE-1, which can thus be considered an inactivator-resistant mutant of P99. However, the second-order rate constant for the inactivation by BAL29880 probably remains adequate for a rather rapid reaction with CHE-1 in the absence of protection by the substrate. Copyright © 2016, American Society for Microbiology. All Rights Reserved.

Citation

Adriana Fernea, Moreno Galleni, Jean-Marie Frère. Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1. Antimicrobial agents and chemotherapy. 2016 Mar;60(3):1747-50

PMID: 26729500

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