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

Samuelsen, O., Castanheira, M., Walsh, Timothy Rutland ORCID: https://orcid.org/0000-0003-4315-4096 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:	Schools > Medicine Research Institutes & Centres > 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:	05 May 2023 18:30
URI:	https://orca.cardiff.ac.uk/id/eprint/27236

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