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Antimicrobial Agents and Chemotherapy, August 2008, p. 2905-2908, Vol. 52, No. 8
0066-4804/08/$08.00+0     doi:10.1128/AAC.00166-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Kinetic Characterization of VIM-7, a Divergent Member of the VIM Metallo-β-Lactamase Family

Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, Tromsø, Norway,¹ Department of Cellular and Molecular Medicine, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, United Kingdom,² Department of Medical Microbiology, University of Cardiff, Heath Park, Cardiff CF14 4XN, United Kingdom,³ JMI Laboratories, North Liberty, Iowa 52317⁴

Received 5 February 2008/ Returned for modification 24 March 2008/ Accepted 4 June 2008

Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activities comparable to those of VIM-2. Cephalosporinase activity was variable and generally lower than those of VIM-1 and VIM-2. A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.

Published ahead of print on 16 June 2008.