Extended-spectrum cephalosporinase in Acinetobacter baumannii.
Article Details
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Rodriguez-Martinez JM, Nordmann P, Ronco E, Poirel L
Extended-spectrum cephalosporinase in Acinetobacter baumannii.
Antimicrob Agents Chemother. 2010 Aug;54(8):3484-8. doi: 10.1128/AAC.00050-10. Epub 2010 Jun 14.
- PubMed ID
- 20547808 [ View in PubMed]
- Abstract
An AmpC-type beta-lactamase conferring high-level resistance to expanded-spectrum cephalosporins and monobactams was characterized from an Acinetobacter baumannii clinical isolate. This class C beta-lactamase (named ADC-33) possessed a Pro210Arg substitution together with a duplication of an Ala residue at position 215 (inside the Omega-loop) compared to a reference AmpC cephalosporinase from A. baumannii. ADC-33 hydrolyzed ceftazidime, cefepime, and aztreonam at high levels, which allows the classification of this enzyme as an extended-spectrum AmpC (ESAC). Site-directed mutagenesis confirmed the role of both substitutions in its ESAC property.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Cefotaxime Beta-lactamase Protein Acinetobacter baumannii UnknownNot Available Details