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

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 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.

authors

Fernea A,Galleni M,Frère JM

doi

10.1128/AAC.02062-15

subject

Has Abstract

pub_date

2016-01-04 00:00:00

pages

1747-50

issue

3

eissn

0066-4804

issn

1098-6596

pii

AAC.02062-15

journal_volume

60

pub_type

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