Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii

Antimicrob Agents Chemother. 2005 Oct;49(10):4174-9. doi: 10.1128/AAC.49.10.4174-4179.2005.

Abstract

A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. beta-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme of A. baumannii and 62 and 56% amino acid identity with the carbapenem-hydrolyzing oxacillinases OXA-24 and OXA-23, respectively. Biochemical characterization of the purified OXA-69 revealed a narrow-spectrum hydrolysis profile but including, at a low level, imipenem and meropenem. By PCR and sequencing bla(OXA-69)-like genes were identified in all A. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter baumannii / drug effects
  • Acinetobacter baumannii / enzymology*
  • Acinetobacter baumannii / genetics
  • Acinetobacter baumannii / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology*
  • Base Sequence
  • Carbapenems / chemistry
  • Carbapenems / pharmacology
  • Cloning, Molecular
  • Dimerization
  • Genes, Bacterial
  • Geography
  • Hydrolysis
  • Kinetics
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Molecular Weight
  • Phylogeny
  • Plasmids
  • Proteins / analysis
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • beta-Lactamases / chemistry*
  • beta-Lactamases / drug effects
  • beta-Lactamases / genetics
  • beta-Lactamases / isolation & purification
  • beta-Lactamases / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Carbapenems
  • Proteins
  • beta-Lactamases
  • oxacillinase

Associated data

  • GENBANK/AY859527
  • GENBANK/AY859528
  • GENBANK/AY859529