Interactions of biapenem with active-site serine and metallo-beta-lactamases

Antimicrob Agents Chemother. 1995 Jun;39(6):1300-5. doi: 10.1128/AAC.39.6.1300.

Abstract

Biapenem, formerly LJC 10,627 or L-627, a carbapenem antibiotic, was studied in its interactions with 12 beta-lactamases belonging to the four molecular classes proposed by R. P. Ambler (Philos. Trans. R. Soc. Lond. Biol. Sci. 289:321-331, 1980). Kinetic parameters were determined. Biapenem was readily inactivated by metallo-beta-lactamases but behaved as a transient inhibitor of the active-site serine enzymes tested, although with different acylation efficiency values. Class A and class D beta-lactamases were unable to confer in vitro resistance toward this carbapenem antibiotic. Surprisingly, the same situation was found in the case of class B enzymes from Aeromonas hydrophila AE036 and Bacillus cereus 5/B/6 when expressed in Escherichia coli strains.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Enterobacteriaceae / drug effects
  • Enterobacteriaceae / enzymology
  • Enzyme Activation
  • Enzyme Inhibitors
  • Imipenem / metabolism
  • Imipenem / pharmacology
  • Kinetics
  • Metalloproteins / metabolism*
  • Microbial Sensitivity Tests
  • Serine / metabolism*
  • Thienamycins / metabolism*
  • Thienamycins / pharmacology
  • Zinc / metabolism
  • beta-Lactam Resistance
  • beta-Lactamases / classification
  • beta-Lactamases / drug effects
  • beta-Lactamases / metabolism*

Substances

  • Enzyme Inhibitors
  • Metalloproteins
  • Thienamycins
  • Serine
  • Imipenem
  • beta-Lactamases
  • Zinc
  • biapenem