{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":73,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["43(6)"],"submitter":["Danel F"],"pubmed_abstract":["Pseudomonas aeruginosa isolates 871 and 873 were isolated at Hacettepe University Hospital in Ankara and were highly resistant to ceftazidime (MIC, 128 microg/ml). Each produced three beta-lactamases, with pIs of 5.3, 6.1, and 7.9. The beta-lactamase with a pI of 5.3 was previously shown to be PER-1 enzyme. The antibiograms of the isolates were not entirely explained by production of PER-1 enzyme, insofar as ceftazidime resistance was incompletely reversed by clavulanate. The enzymes with pIs of 6.1 and 7.9 were therefore investigated. The enzyme with a pI of 6.1 proved to be a novel mutant of OXA-10, which we designated OXA-17, and had asparagine changed to serine at position 73 of the protein. When cloned into Escherichia coli XL1-blue, OXA-17 enzyme conferred greater resistance to cefotaxime, latamoxef, and cefepime than did OXA-10, but it had only a marginal (two- to fourfold) effect on the MIC of ceftazidime. This behavior contrasted with that of previous OXA-10 mutants, specifically OXA-11, -14, and -16, which predominately compromise ceftazidime. Extracted OXA-17 enzyme had relatively greater activity than OXA-10 against oxacillin, cloxacillin, and cefotaxime but, in terms of kcat/Km, it had lower catalytic efficiency against most beta-lactams. The enzyme with a pI of 7.9 was shown by gene sequencing to be OXA-2."],"journal":["Antimicrobial agents and chemotherapy"],"pagination":["1362-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC89279"],"repository":["biostudies-literature"],"pubmed_title":["OXA-17, a further extended-spectrum variant of OXA-10 beta-lactamase, isolated from Pseudomonas aeruginosa."],"pmcid":["PMC89279"],"pubmed_authors":["Duke B","Hall LM","Danel F","Gur D","Livermore DM"],"view_count":["73"],"additional_accession":[]},"is_claimable":false,"name":"OXA-17, a further extended-spectrum variant of OXA-10 beta-lactamase, isolated from Pseudomonas aeruginosa.","description":"Pseudomonas aeruginosa isolates 871 and 873 were isolated at Hacettepe University Hospital in Ankara and were highly resistant to ceftazidime (MIC, 128 microg/ml). Each produced three beta-lactamases, with pIs of 5.3, 6.1, and 7.9. The beta-lactamase with a pI of 5.3 was previously shown to be PER-1 enzyme. The antibiograms of the isolates were not entirely explained by production of PER-1 enzyme, insofar as ceftazidime resistance was incompletely reversed by clavulanate. The enzymes with pIs of 6.1 and 7.9 were therefore investigated. The enzyme with a pI of 6.1 proved to be a novel mutant of OXA-10, which we designated OXA-17, and had asparagine changed to serine at position 73 of the protein. When cloned into Escherichia coli XL1-blue, OXA-17 enzyme conferred greater resistance to cefotaxime, latamoxef, and cefepime than did OXA-10, but it had only a marginal (two- to fourfold) effect on the MIC of ceftazidime. This behavior contrasted with that of previous OXA-10 mutants, specifically OXA-11, -14, and -16, which predominately compromise ceftazidime. Extracted OXA-17 enzyme had relatively greater activity than OXA-10 against oxacillin, cloxacillin, and cefotaxime but, in terms of kcat/Km, it had lower catalytic efficiency against most beta-lactams. The enzyme with a pI of 7.9 was shown by gene sequencing to be OXA-2.","dates":{"release":"1999-01-01T00:00:00Z","publication":"1999 Jun","modification":"2024-11-15T22:41:45.938Z","creation":"2019-03-27T00:18:25Z"},"accession":"S-EPMC89279","cross_references":{"pubmed":["10348753"],"doi":["10.1128/AAC.43.6.1362"]}}