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Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N(132)G in the Conserved SDN Motif
The substitution N(132)G 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...
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| Publicado en: | Antimicrob Agents Chemother |
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| Autores principales: | , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology
2017
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5328567/ https://ncbi.nlm.nih.gov/pubmed/28069651 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AAC.02510-16 |
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