OXA-35 is an OXA-10-related beta-lactamase from Pseudomonas aeruginosa
Author(s) -
Dominique Aubert
Publication year - 2001
Publication title -
journal of antimicrobial chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.124
H-Index - 194
eISSN - 1460-2091
pISSN - 0305-7453
DOI - 10.1093/jac/48.5.717
Subject(s) - aztreonam , imipenem , cefsulodin , ceftazidime , pseudomonas aeruginosa , cefepime , microbiology and biotechnology , beta lactamase , cloxacillin , chemistry , biology , antibiotics , bacteria , biochemistry , penicillin , genetics , escherichia coli , gene
Pseudomonas aeruginosa clinical isolate PA35 is resistant to amino- and ureido-penicillins, has intermediate susceptibility to cefsulodin, cefepime and aztreonam, and is susceptible to imipenem and ceftazidime. Cloning and sequencing revealed a new beta-lactamase variant, OXA-35, sharing 96% amino acid identity with OXA-10. OXA-35 displays a restricted-substrate hydrolysis profile with improved hydrolysis of amoxicillin and cloxacillin compared with OXA-10. OXA-35 differs from derivatives OXA-19 and OXA-28 by one amino acid substitution and may be a progenitor of these OXA-13-like extended-spectrum beta-lactamases.
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