Effects of Ser130Gly and Asp240Lys Substitutions in Extended-Spectrum β-Lactamase CTX-M-9-Reference-Cited by-同舟云学术

Effects of Ser130Gly and Asp240Lys Substitutions in Extended-Spectrum β-Lactamase CTX-M-9

Published:2003-09 Issue:9 Volume:47 Page:2958-2961
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Aumeran C.¹,Chanal C.¹,Labia R.²,Sirot D.¹,Sirot J.¹,Bonnet R.¹

Affiliation:

1. Laboratoire de Bactériologie, Faculté de Médecine, 63001 Clermont-Ferrand, Cedex

2. UMR 175, CNRS-MNHN, 29000 Quimper, France

Abstract

ABSTRACT In CTX-M-9 extended-spectrum β-lactamases (ESBLs), an S130G mutation induced a 40- to 650-fold increase in 50% inhibitory concentrations but decreased hydrolytic activity against cefotaxime. A D240K mutation did not modify enzymatic efficiency against ceftazidime. Residue K240 could interact with Q270 and therefore not with ceftazidime, in contrast with what was observed with certain TEM/SHV-type ESBLs.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.47.9.2958-2961.2003

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