Binding of latamoxef (moxalactam) and its decarboxylated derivative toEscherichia coli andPseudomonas aeruginosa penicillin-binding proteins

Publisher Website
Google Scholar
Abstract
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 123I-radiolabelled pemcillin X. atarnoxef and the decarboxylated derivative were highly bound to most of the PBPs, ith the exception of PBP-2. As the two compounds possess a phenolic sidechain, hey also could be radiolabelled with 123I. The proteins thus labelled by these derivahves were qualitatively the same as those labelled by 123I-penicillin X, except for BP-2 which was not labelled by the iodo denvatives of latamoxef and its dccarboxylated derivahve, and PBP-lc (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. hus, it was concluded that the carboxylic group of latamoxef does not play an important role in affinity for the targets.

This publication has 12 references indexed in Scilit: