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. 1988 Aug;32(8):1243–1246. doi: 10.1128/aac.32.8.1243

Novel plasmid-mediated beta-lactamase from Escherichia coli that inactivates oxyimino-cephalosporins.

Y Matsumoto 1, F Ikeda 1, T Kamimura 1, Y Yokota 1, Y Mine 1
PMCID: PMC172385  PMID: 3056257

Abstract

A highly cephem-resistant Escherichia coli strain, FP1546, isolated from the fecal flora of laboratory dogs previously administered beta-lactam antibiotics was found to produce a beta-lactamase, FEC-1, of 48-kilodalton size and pI 8.2. FEC-1 hydrolyzed cefuroxime, cefotaxime, cefmenoxime, and ceftriaxone, as well as the enzymatically less-stable antibiotics cephaloridine, cefotiam, and cefpiramide. Of the oxyimino-cephalosporins, ceftizoxime was fairly stable to FEC-1. FEC-1 differed notably from chromosomal E. coli cephalosporinase, especially in its broad-spectrum substrate profile and its high inhibition by clavulanic acid, sulbactam, and imipenem. A conjugation study revealed that FEC-1 was encoded by a 74-megadalton plasmid, pFCX1. This may be the first instance of a plasmid-mediated oxyimino-cephalosporinase from E. coli.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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