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http://purl.uniprot.org/citations/9687391http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9687391http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9687391http://www.w3.org/2000/01/rdf-schema#comment"We determined the nucleotide sequences of blaCARB-4 encoding CARB-4 and deduced a polypeptide of 288 amino acids. The gene was characterized as a variant of group 2c carbenicillin-hydrolyzing beta-lactamases such as PSE-4, PSE-1, and CARB-3. The level of DNA homology between the bla genes for these beta-lactamases varied from 98.7 to 99.9%, while that between these genes and blaCARB-4 encoding CARB-4 was 86.3%. The blaCARB-4 gene was acquired from some other source because it has a G+C content of 39.1%, compared to a G+C content of 67% for typical Pseudomonas aeruginosa genes. DNA sequencing revealed that blaAER-1 shared 60.8% DNA identity with blaPSE-3 encoding PSE-3. The deduced AER-1 beta-lactamase peptide was compared to class A, B, C, and D enzymes and had 57.6% identity with PSE-3, including an STHK tetrad at the active site. For CARB-4 and AER-1, conserved canonical amino acid boxes typical of class A beta-lactamases were identified in a multiple alignment. Analysis of the DNA sequences flanking blaCARB-4 and blaAER-1 confirmed the importance of gene cassettes acquired via integrons in bla gene distribution."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.org/dc/terms/identifier"doi:10.1128/aac.42.8.1966"xsd:string
http://purl.uniprot.org/citations/9687391http://purl.org/dc/terms/identifier"doi:10.1128/aac.42.8.1966"xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Levesque R.C."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Levesque R.C."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Sanschagrin F."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Sanschagrin F."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Bejaoui N."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/author"Bejaoui N."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/name"Antimicrob. Agents Chemother."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/name"Antimicrob. Agents Chemother."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/pages"1966-1972"xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/pages"1966-1972"xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/title"Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing beta-lactamases."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/title"Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing beta-lactamases."xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/9687391http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/9687391http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9687391
http://purl.uniprot.org/citations/9687391http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9687391
http://purl.uniprot.org/citations/9687391http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9687391
http://purl.uniprot.org/citations/9687391http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9687391