Kinetic Characterization of VIM-7, a Divergent Member of the VIM Metallo-β-Lactamase Family-Reference-Cited by-同舟云学术

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

Published:2008-08 Issue:8 Volume:52 Page:2905-2908
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Samuelsen Ørjan¹²,Castanheira Mariana²³,Walsh Timothy R.⁴,Spencer James²

Affiliation:

1. Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, Tromsø, Norway

2. Department of Cellular and Molecular Medicine, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, United Kingdom

3. JMI Laboratories, North Liberty, Iowa 52317

4. Department of Medical Microbiology, University of Cardiff, Heath Park, Cardiff CF14 4XN, United Kingdom

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.00166-08

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