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Antimicrobial Agents and Chemotherapy, June 2008, p. 2250-2252, Vol. 52, No. 6
0066-4804/08/$08.00+0     doi:10.1128/AAC.01025-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Biochemical Characterization of Metallo-β-Lactamase VIM-11 from a Pseudomonas aeruginosa Clinical Strain ^,

Patricia Marchiaro,^1, Pablo E. Tomatis,^2, María A. Mussi,¹ Fernando Pasteran,³ Alejandro M. Viale,¹ Adriana S. Limansky,¹ and Alejandro J. Vila^2*

Departamento de Microbiología,¹ Departamento de Química Biológica, Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Buenos Aires, Argentina,² Servicio Antimicrobianos, Departamento Bacteriología, Instituto Nacional de Enfermedades Infecciosas—ANLIS Dr. Carlos G. Malbrán, Ciudad Autónoma de Buenos Aires, Buenos Aires, Argentina³

Received 3 August 2007/ Returned for modification 12 October 2007/ Accepted 15 March 2008

A detailed biochemical characterization of the Pseudomonas aeruginosa VIM-11 metallo-β-lactamase (MβL) is reported. The only substitution differentiating VIM-11 from VIM-2 (N165S) promoted a slightly improved catalytic efficiency of the former on 3 out of 12 substrates, notably the bulky cephalosporins. Thus, MβL-mediated resistance also may be modulated by remote mutations.

Published ahead of print on 24 March 2008.

Supplemental material for this article may be found at http://aac.asm.org/.

These authors contributed equally to this work.

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