Journal of Antimicrobial Chemotherapy, Vol 41, 115-118, Copyright © 1998 by The British Society for Antimicrobial Chemotherapy
GS Babini, F Danel, SD Munro, PA Micklesen and DM Livermore
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.
ORIGINAL ARTICLES
Unusual tazobactam-sensitive AmpC beta-lactamase from two Escherichia coli isolates
Department of Medical Microbiology, St Bartholomew's, London, UK.
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