Unusual tazobactam-sensitive AmpC beta-lactamase from two Escherichia coli isolates | Zendy

G Babini | Zendy; Franck Danel | Zendy; Stephen Munro | Zendy; P A Micklesen | Zendy; David M. Livermore | Zendy

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Unusual tazobactam-sensitive AmpC beta-lactamase from two Escherichia coli isolates

Author(s) -

G Babini,

Franck Danel,

Stephen Munro,

P A Micklesen,

David M. Livermore

Publication year - 1998

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/41.1.115

Subject(s) - ceftazidime , escherichia coli , cephaloridine , tazobactam , microbiology and biotechnology , beta lactamase inhibitors , beta lactamase , biology , cephalosporin , enterobacteriaceae , enzyme , antibiotics , chemistry , bacteria , biochemistry , imipenem , antibiotic resistance , genetics , gene , pseudomonas aeruginosa

Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC beta-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified beta-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin.

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