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Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N132G in the Conserved SDN Motif.

Antimicrobial agents and chemotherapy - 1 Mar 2017

Ourghanlian Clément, Soroka Daria, Arthur Michel

Abstract excerpt

The substitution N132G in the SDN motif of class A β-lactamases from rapidly growing mycobacteria was previously shown to impair their inhibition by avibactam but to improve the stability of acyl-enzymes formed with clavulanate. The same substitution was introduced in KPC-2 and CTX-M-15 to assess its impact on β-lactamases from Enterobacteriaceae and evaluate whether it may lead to resistance to the...

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Identifiers

PMID: 28069651
DOI: 10.1128/AAC.02510-16
PMCID: PMC5328567

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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