Binding of Latamoxef (Moxalactam) and Its Decarboxylated Derivative to Escherichia Coli and Pseudomonas Aeruginosa Penicillin-Binding Proteins

J Antimicrob Chemother. 1985 Jan;15(1):9-15. doi: 10.1093/jac/15.1.9.


The binding of latamoxef (moxalactam) and of a decarboxylated derivative to Escherichia coli and Pseudomonas aeruginosa penicillin-binding proteins (PBPs) was measured by competition experiments with 125I-radiolabelled penicillin X. Latamoxef and the decarboxylated derivative were highly bound to most of the PBPs, with the exception of PBP-2. As the two compounds possess a phenolic side-chain, they also could be radiolabelled with 125I. The proteins thus labelled by these derivatives were qualitatively the same as those labelled by 125I-penicillin X, except for PBP-2 which was not labelled by the iodo derivatives of latamoxef and its decarboxylated derivative, and PBP-1c (in E. coli) which is labelled only poorly by the radioactive penicillin. No important difference between latamoxef and its decarboxylated derivative was found, and the same observation was made for penicillin G and carbenicillin. Thus, it was concluded that the carboxylic group of latamoxef does not play an important role in affinity for the targets.

MeSH terms

  • Bacterial Proteins*
  • Carboxypeptidases / metabolism*
  • Carrier Proteins / metabolism*
  • Decarboxylation
  • Escherichia coli / metabolism*
  • Hexosyltransferases*
  • Iodine Radioisotopes
  • Moxalactam / metabolism*
  • Muramoylpentapeptide Carboxypeptidase / metabolism*
  • Penicillin-Binding Proteins
  • Penicillins / metabolism
  • Peptidyl Transferases*
  • Pseudomonas aeruginosa / metabolism*
  • Structure-Activity Relationship


  • Bacterial Proteins
  • Carrier Proteins
  • Iodine Radioisotopes
  • Penicillin-Binding Proteins
  • Penicillins
  • Peptidyl Transferases
  • Hexosyltransferases
  • Carboxypeptidases
  • Muramoylpentapeptide Carboxypeptidase
  • Moxalactam