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Antimicrobial Agents and Chemotherapy, January 2009, p. 323-326, Vol. 53, No. 1
0066-4804/09/$08.00+0 doi:10.1128/AAC.00608-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Service de Bactériologie-Hygiène, Centre hospitalier universitaire d'Amiens, Hôpital Nord, 80000 Amiens, France,1 Service de Bactériologie-Virologie-Hygiène, Unité INSERM 914 Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris Sud, 94275 le K.-Bicêtre, France,2 Center for Protein Engineering, Université de Liège, Liège B-4000, Belgium3
Received 8 May 2008/ Returned for modification 10 August 2008/ Accepted 3 November 2008
Two AmpC variants harboring the S287N substitution were obtained by mutagenesis from cephalosporinases representative of the phylogenetic groups A and B2 of Escherichia coli. Their biochemical characterization revealed that the S287N replacement led to an important increase in the catalytic efficiency toward extended-spectrum cephalosporins in the AmpC β-lactamase of group A only.
Published ahead of print on 10 November 2008.
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