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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Unusual tazobactam-sensitive AmpC beta-lactamase from two Escherichia coli isolates. Babini, G.S., Danel, F., Munro, S.D., Micklesen, P.A., Livermore, D.M. J. Antimicrob. Chemother. (1998) [Pubmed]
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