A kinetic study on the interaction between tazobactam (a penicillanic acid sulphone derivative) and active-site serine beta-lactamases

J Enzyme Inhib. 2000;15(1):1-10.

Abstract

The interaction between tazobactam and several chromosome- and plasmid-encoded (TEM, SHV, PSE types) class A and C beta-lactamases was studied by spectrophotometry. Tazobactam behaved as a competitive inhibitor or inactivator able to restore in several cases the efficiency of piperacillin as a partner beta-lactam. A detailed kinetic analysis permitted measurement of the acylation efficiency for some cephalosporinases and broad-spectrum beta-lactamases; the presence of a turn-over of acyl-enzyme complex was also evaluated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter / drug effects
  • Acinetobacter / enzymology
  • Binding Sites
  • Citrobacter / drug effects
  • Citrobacter / enzymology
  • Enzyme Inhibitors / pharmacokinetics
  • Enzyme Inhibitors / pharmacology
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology
  • Kinetics
  • Klebsiella pneumoniae / drug effects
  • Klebsiella pneumoniae / enzymology
  • Microbial Sensitivity Tests
  • Morganella / drug effects
  • Morganella / enzymology
  • Mycobacterium fortuitum / drug effects
  • Mycobacterium fortuitum / enzymology
  • Penicillanic Acid / analogs & derivatives*
  • Penicillanic Acid / pharmacokinetics
  • Penicillanic Acid / pharmacology
  • Providencia / drug effects
  • Providencia / enzymology
  • Pseudomonas aeruginosa / drug effects
  • Pseudomonas aeruginosa / enzymology
  • Serine*
  • Serratia marcescens / drug effects
  • Serratia marcescens / enzymology
  • Tazobactam
  • beta-Lactamase Inhibitors*
  • beta-Lactamases / chemistry*
  • beta-Lactamases / genetics

Substances

  • Enzyme Inhibitors
  • beta-Lactamase Inhibitors
  • Serine
  • Penicillanic Acid
  • beta-Lactamases
  • Tazobactam