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http://purl.uniprot.org/citations/10817708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10817708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10817708http://www.w3.org/2000/01/rdf-schema#comment"Acinetobacter baumannii RYC 52763/97, a clinical isolate involved in a prolonged nosocomial outbreak at our hospital, was resistant to all beta-lactams tested, including imipenem and meropenem, which had MICs of 128 and 256 microg/ml, respectively. This strain synthesized three beta-lactamases: a plasmid-mediated TEM-1 beta-lactamase (pI 5.4), an AmpC-type chromosomal cephalosporinase (pI 9.4), and a novel, presumptively chromosomally mediated OXA-related enzyme (pI 9.0) named OXA-24. After cloning and sequencing, the deduced amino acid sequence of the OXA-24 beta-lactamase showed 40% homology with the OXA-10 (PSE-2) and OXA-7 beta-lactamases, 39% homology with the OXA-11 and OXA-5 enzymes, and 33% homology with the LCR-1 beta-lactamase. The amino acid sequence of the OXA-24 beta-lactamase contained the STFK motif found in serine beta-lactamases, but the typical class D triad KTG was replaced by KSG and the motif YGN was replaced by FGN. The OXA-24 beta-lactamase hydrolyzed benzylpenicillin and cephaloridine but lacked activity against oxacillin, cloxacillin, and methicillin. The enzymatic activity was inhibited by chloride ions and by tazobactam (50% inhibitory concentration [IC(50)], 0.5 microM), sulbactam (IC(50), 40 microM), and clavulanic acid (IC(50), 50 microM). Carbapenem MICs for an Escherichia coli transformant (pBMB-1) expressing the cloned OXA-24 enzyme had a fourfold increase. Relative V(max)/K(m) values of 13 and 6 were obtained with imipenem and meropenem, respectively, and a positive microbiological assay result with imipenem was obtained with a purified enzymatic extract of this transformant strain. Therefore, we consider this new beta-lactamase to be involved in the carbapenem resistance of A. baumannii RYC 52763/97."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.org/dc/terms/identifier"doi:10.1128/AAC.44.6.1556-1561.2000"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.org/dc/terms/identifier"doi:10.1128/aac.44.6.1556-1561.2000"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Bou G."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Bou G."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Oliver A."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Oliver A."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Martinez-Beltran J."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/author"Martinez-Beltran J."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/name"Antimicrob. Agents Chemother."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/name"Antimicrob Agents Chemother"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/pages"1556-1561"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/pages"1556-1561"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/title"OXA-24, a novel class D beta-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/title"OXA-24, a novel class D beta-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain."xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/10817708http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/10817708http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10817708
http://purl.uniprot.org/citations/10817708http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10817708
http://purl.uniprot.org/citations/10817708http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10817708
http://purl.uniprot.org/citations/10817708http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10817708