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. 1998 Jan;41(1):115-8.
doi: 10.1093/jac/41.1.115.

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

G S Babini  1 , F Danel, S D Munro, P A Micklesen, D M Livermore
Affiliations

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

G S Babini et al. J Antimicrob Chemother. 1998 Jan.

Abstract

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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