PMID:3298212

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Citation

Kraus, W and Höltje, JV (1987) Two distinct transpeptidation reactions during murein synthesis in Escherichia coli. J. Bacteriol. 169:3099-103

Abstract

Murein synthesized in ether-permeabilized cells of Escherichia coli deficient in individual penicillin-binding proteins (PBPs) and in the presence of certain beta-lactam antibiotics was analyzed by high-pressure liquid chromatography separation of the muramidase split products. PBP 1b was found to to be the major murein synthesizing activity that was poorly compensated for by PBP 1a. A PBP 2 mutant as well as mecillinam-inhibited cells showed increased activity in the formation of oligomeric muropeptides as well as UDP-muramylpeptidyl-linked muropeptides, the reaction products of transpeptidation, bypassing the lipid intermediate. In contrast, penicillin G and furazlocillin severely inhibited these reactions but stimulated normal dimer production. It is concluded that two distinct transpeptidases exist in E. coli: one, highly sensitive to penicillin G and furazlocillin, catalyzes the formation of hyper-cross-linked muropeptides, and a second one, quite resistant to these antibiotics, synthesizes muropeptide dimers.

Links

PubMed PMC212355

Keywords

Amdinocillin/pharmacology; Azlocillin/analogs & derivatives; Azlocillin/pharmacology; Bacterial Proteins; Carrier Proteins/physiology; Cell Division; Escherichia coli/growth & development; Escherichia coli/metabolism; Hexosyltransferases; Imidazolidines; Muramoylpentapeptide Carboxypeptidase/physiology; Penicillin-Binding Proteins; Penicillins/pharmacology; Peptidoglycan/biosynthesis; Peptidyl Transferases/metabolism

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