TEM-89 beta-lactamase produced by a Proteus mirabilis clinical isolate: new complex mutant (CMT 3) with mutations in both TEM-59 (IRT-17) and TEM-3

Antimicrob Agents Chemother. 2001 Dec;45(12):3591-4. doi: 10.1128/AAC.45.12.3591-3594.2001.

Abstract

TEM-89 (CMT-3) is the first complex mutant beta-lactamase produced by a clinical strain of Proteus mirabilis (strain Pm 631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM beta-lactamase IRT-17): Ser-130 to Gly. TEM-89 hydrolyzed penicillins to the same extent that TEM-3 did but lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors.

MeSH terms

  • Amino Acid Substitution
  • Conjugation, Genetic
  • Escherichia coli / genetics
  • Humans
  • Isoelectric Focusing
  • Kinetics
  • Molecular Sequence Data
  • Mutation / genetics
  • Plasmids / genetics
  • Proteus Infections / microbiology*
  • Proteus mirabilis / drug effects
  • Proteus mirabilis / enzymology*
  • Proteus mirabilis / genetics*
  • Reverse Transcriptase Polymerase Chain Reaction
  • beta-Lactamases / genetics*
  • beta-Lactamases / metabolism*

Substances

  • TEM-89 beta-lactamase
  • beta-Lactamases

Associated data

  • GENBANK/AY039040