Chromogenic depsipeptide substrates for beta-lactamases and penicillin-sensitive DD-peptidases

Biochem J. 1990 Sep 1;270(2):525-9. doi: 10.1042/bj2700525.

Abstract

Various ester and thioester derivatives of hippuric acid have been prepared which were substrates of both beta-lactamases and DD-peptidases. The thioesters were more rapidly hydrolysed by nearly all the enzymes. Surprisingly, the enzymes acted rather efficiently on substrates which did not contain any chiral centre.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Chromogenic Compounds / metabolism*
  • Esters
  • Hydrolysis
  • Kinetics
  • Molecular Sequence Data
  • Molecular Structure
  • Muramoylpentapeptide Carboxypeptidase / metabolism*
  • Oligopeptides / metabolism*
  • Penicillins / pharmacology*
  • Pronase / metabolism
  • Substrate Specificity
  • beta-Lactamases / metabolism*

Substances

  • Chromogenic Compounds
  • Esters
  • Oligopeptides
  • Penicillins
  • Muramoylpentapeptide Carboxypeptidase
  • Pronase
  • beta-Lactamases