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. 2015 Mar;59(3):1755-8.
doi: 10.1128/AAC.03843-14. Epub 2014 Dec 15.

Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidis

Luisa Borgianni  1 , Filomena De Luca  1 , Maria Cristina Thaller  2 , Yunsop Chong  3 , Gian Maria Rossolini  4 , Jean-Denis Docquier  5
Affiliations

Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidis

Luisa Borgianni et al. Antimicrob Agents Chemother. 2015 Mar.

Abstract

The POM-1 metallo-β-lactamase is a subclass B3 resident enzyme produced by Pseudomonas otitidis, a pathogen causing otic infections. The enzyme was overproduced in Escherichia coli BL21(DE3), purified by chromatography, and subjected to structural and functional analysis. The purified POM-1 is a tetrameric enzyme of broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins.

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