Biochemical characterization of laboratory mutants of extended-spectrum beta-lactamase TEM-60

Antimicrob Agents Chemother. 2004 Sep;48(9):3579-82. doi: 10.1128/AAC.48.9.3579-3582.2004.

Abstract

Three mutants of the extended-spectrum beta-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • DNA Primers
  • Enzyme Inhibitors / pharmacology
  • Escherichia coli / genetics
  • Kinetics
  • Mutagenesis, Site-Directed
  • Mutation / genetics*
  • Reverse Transcriptase Polymerase Chain Reaction
  • beta-Lactam Resistance
  • beta-Lactamases / genetics*

Substances

  • DNA Primers
  • Enzyme Inhibitors
  • beta-Lactamases
  • beta-lactamase TEM-60, Providencia stuartii