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.

Borgianni, L., DE LUCA, F., Thaller, M.C., Chong, Y., Rossolini, G.M., Docquier, J.D. (2015). Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidis. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 59(3), 1755-1758 [10.1128/AAC.03843-14].

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

BORGIANNI, LUISA;DE LUCA, FILOMENA;ROSSOLINI, GIAN MARIA;DOCQUIER, JEAN DENIS
2015-01-01

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.
Borgianni, L., DE LUCA, F., Thaller, M.C., Chong, Y., Rossolini, G.M., Docquier, J.D. (2015). Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidis. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 59(3), 1755-1758 [10.1128/AAC.03843-14].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/1008812
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