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Antimicrobial Agents and Chemotherapy, September 2003, p. 2958-2961, Vol. 47, No. 9
0066-4804/03/$08.00+0     DOI: 10.1128/AAC.47.9.2958-2961.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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

Laboratoire de Bactériologie, Faculté de Médecine, 63001 Clermont-Ferrand, Cedex,¹ UMR 175, CNRS-MNHN, 29000 Quimper, France²

Received 17 April 2003/ Returned for modification 23 May 2003/ Accepted 4 June 2003

In CTX-M-9 extended-spectrum ß-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.

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