Beta-lactamase stability and inhibitory activity of meropenem combined with a potent antibacterial activity

H. Nouda, E. T. Harabe, Y. Sumita, T. Okuda, M. Fukasawa

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


The affinity of meropenem for various known types of β-lactamases and its stability to them were tested in comparison with other β-lactams, including imipenem. Meropenem exhibited a marked stability to all β-lactamases tested and was only hydrolyzed by Xanthomonas maltophilia β-lactamase, as were other β-lactams. This was responsible for the potent antibacterial activities of meropenem against β-lactamase-producing strains. Meropenem and imipenem had almost the same, relatively high affinity for β-lactamases; however, they had a lower affinity than clavulanic acid for penicillin β-lactamases and cefoxitin for cephalosporin β-lactamases. Meropenem also had higher β-lactamase inhibitory activity than imipenem. Meropenem inhibited type III (TEM-1), Ia Citrobacter freundii and Ic Proteus vulgaris β-latamases in a progressive manner. Meropenem was thought to be a potent inhibitor of various β-lactamase because of its ability to form stable enzyme-meropenem acyl-complexes. Meropenem generally exhibited a lower induction potential than imipenem against five clinical isolates of C. freundii, Enterobacter cloacae and Pseudomonas aeruginosa, but its induction potential was higher than that of ceftazidime. Meropenem induced, β-lactamases at concentrations above the MIC.

Original languageEnglish
Pages (from-to)218-224
Number of pages7
Issue number4
Publication statusPublished - 1992


  • B-lactamase induction
  • Meropenem
  • β-lactamase inhibition
  • β-lactamase stability

ASJC Scopus subject areas

  • Oncology
  • Pharmacology
  • Drug Discovery
  • Pharmacology (medical)
  • Infectious Diseases


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