DD-peptidases and beta-lactamases: catalytic mechanisms and specificities

J Chemother. 1995 Feb;7(1):3-7. doi: 10.1179/joc.1995.7.1.3.

Abstract

DD-peptidases and beta-lactamases share several common properties, including the formation of an acylenzyme intermediate in their catalytic pathways. In their interactions with beta-lactam antibiotics, the stability of this intermediate is much higher with the peptidases than with the beta-lactamases. The structural factors responsible for this difference have not been identified. The evolution of beta-lactamases is taking place before our eyes, since mutants are constantly selected which can hydrolyze the molecules newly introduced as "beta-lactamase resistant" in the chemotherapeutic arsenal.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Catalysis
  • Molecular Sequence Data
  • Muramoylpentapeptide Carboxypeptidase / metabolism*
  • Protein Conformation
  • Substrate Specificity
  • beta-Lactamases / metabolism*

Substances

  • Muramoylpentapeptide Carboxypeptidase
  • beta-Lactamases