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
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Research Support, Non-U.S. Gov't
MeSH terms
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Acinetobacter baumannii / drug effects
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Acinetobacter baumannii / enzymology*
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Acinetobacter baumannii / genetics
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Acinetobacter baumannii / metabolism
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Amino Acid Motifs
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Amino Acid Sequence
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology*
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Base Sequence
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Carbapenems / chemistry
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Carbapenems / pharmacology
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Cloning, Molecular
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Dimerization
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Genes, Bacterial
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Geography
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Hydrolysis
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Kinetics
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Molecular Weight
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Phylogeny
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Plasmids
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Proteins / analysis
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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beta-Lactamases / chemistry*
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beta-Lactamases / drug effects
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beta-Lactamases / genetics
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beta-Lactamases / isolation & purification
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beta-Lactamases / pharmacology*
Substances
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Anti-Bacterial Agents
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Carbapenems
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Proteins
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beta-Lactamases
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oxacillinase
Associated data
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GENBANK/AY859527
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GENBANK/AY859528
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GENBANK/AY859529