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Kinetic characterization of VIM-7, a divergent member of the VIM metallo-β-lactamase family

Samuelsen, O., Castanheira, M., Walsh, Timothy Rutland and Spencer, J. 2008. Kinetic characterization of VIM-7, a divergent member of the VIM metallo-β-lactamase family. Antimicrobial Agents and Chemotherapy 52 (8) , pp. 2905-2908. 10.1128/AAC.00166-08

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Systems Immunity Research Institute (SIURI)
Subjects: Q Science > QR Microbiology
Additional Information: Pdf uploaded in accordance with publisher's policy at http://www.sherpa.ac.uk/romeo/issn/0066-4804/ (accessed 24/02/2014)
Publisher: American Society for Microbiology
ISSN: 0066-4804
Date of First Compliant Deposit: 30 March 2016
Last Modified: 04 Jun 2017 03:48
URI: http://orca.cf.ac.uk/id/eprint/27236

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Cited 23 times in Scopus. View in Scopus. Powered By Scopus® Data

Cited 18 times in Web of Science. View in Web of Science.

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