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Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.

ABSTRACT: A detailed biochemical characterization of the Pseudomonas aeruginosa VIM-11 metallo-beta-lactamase (MbetaL) 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, MbetaL-mediated resistance also may be modulated by remote mutations.

SUBMITTER: Marchiaro P

PROVIDER: S-EPMC2415757 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.

Marchiaro Patricia P Tomatis Pablo E PE Mussi María A MA Pasteran Fernando F Viale Alejandro M AM Limansky Adriana S AS Vila Alejandro J AJ

Antimicrobial agents and chemotherapy 20080324 6

A detailed biochemical characterization of the Pseudomonas aeruginosa VIM-11 metallo-beta-lactamase (MbetaL) 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, MbetaL-mediated resistance also may be modulated by remote mutations. ...[more]

PMID: 18362187

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Carbapenem-resistant Pseudomonas aeruginosa-carrying VIM-2 metallo-beta-lactamase determinants, Croatia.

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