Beta-lactamase stability of imipenem

J Antimicrob Chemother. 1986 Dec:18 Suppl E:1-8. doi: 10.1093/jac/18.supplement_e.1.

Abstract

The beta-lactamase stability and interactions of imipenem were analysed in comparison with those of cefazolin, cefuroxime, cefoxitin, cefotaxime, ceftazidime, mezlocillin, piperacillin and penicillin G for a set of representative beta-lactamases. These enzymes included penicillinases such as those obtained from Staphylococcus aureus, Escherichia coli and other Enterobacteriaceae (TEM-1 and similar enzymes) (group A); cephalosporinases produced by Esch. coli (Amp C type), Serratia liquefaciens, Enterobacter cloacae, Pseudomonas aeruginosa (group B); and beta-lactamases produced by Klebsiella spp., Proteus vulgaris and Bacteroides fragilis and with a high hydrolytic activity for the newer cephalosporins (group C). Enzymes of group A were demonstrated to be highly active against penicillins and also against the early cephalosporins; enzymes of group B showed hydrolytic activity for all other tested compounds, including the newer cephalosporins and cephamycins, but not imipenem, whereas enzymes of group C were highly active against the new cephalosporins but not against cephamycins and imipenem. In conclusion, imipenem shows a moderate affinity for all these enzymes but no detectable hydrolysis.

MeSH terms

  • Enzyme Stability
  • Gram-Negative Bacteria / enzymology
  • Hydrolysis
  • Imipenem
  • Kinetics
  • Thienamycins / metabolism*
  • Thienamycins / pharmacology
  • beta-Lactamases / metabolism*

Substances

  • Thienamycins
  • Imipenem
  • beta-Lactamases