Effect of various analogues of D-glutamic acid on the D-glutamate-adding enzyme from Escherichia coli

FEMS Microbiol Lett. 1994 Jan 15;115(2-3):223-8. doi: 10.1111/j.1574-6968.1994.tb06642.x.

Abstract

Twenty-four analogues of D-glutamic acid were tested as substrates or inhibitors of the D-glutamate-adding enzyme from Escherichia coli. The best substrates were, in decreasing order of specific activity, D-erythro-4-methylglutamic acid, D-erythro-3-methylglutamic acid, DL-homocysteic acid, (+/-)-trans-1-amino-3-carboxy-cyclopentanecarboxylic acid and (+/-)-trans-1-amino-3-carboxy-cyclohexanecarboxylic acid. Among the different stereoisomers, only the D-erythro isomers for methylglutamic acids, and the trans isomers for the cyclic analogs, were substrates. Apart from the D-erythro-3- and 4-methylglutamic acids and DL-homocysteic acid, none of the examined compounds significantly inhibited the addition of radioactive D-glutamic acid to UDP-N-acetylmuramyl-L-alanine.

Publication types

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

MeSH terms

  • Escherichia coli / enzymology*
  • Glutamates / chemistry*
  • Glutamic Acid
  • Peptide Synthases / antagonists & inhibitors
  • Peptide Synthases / metabolism*
  • Peptidoglycan / biosynthesis
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Glutamates
  • Peptidoglycan
  • Glutamic Acid
  • Peptide Synthases
  • UDP-N-acetylmuramoylalanine-D-glutamate ligase