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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / pharmacology*
  • Carbapenems / pharmacology
  • Catalysis
  • Cephalosporins / pharmacology
  • Escherichia coli / metabolism
  • Penicillins / pharmacology
  • Pseudomonas / enzymology*
  • Pseudomonas / metabolism*
  • beta-Lactamases / metabolism*
  • beta-Lactamases / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carbapenems
  • Cephalosporins
  • Penicillins
  • beta-Lactamases