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. 1997 Oct;179(19):6005–6009. doi: 10.1128/jb.179.19.6005-6009.1997

The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate.

M Adam 1, C Fraipont 1, N Rhazi 1, M Nguyen-Distèche 1, B Lakaye 1, J M Frère 1, B Devreese 1, J Van Beeumen 1, Y van Heijenoort 1, J van Heijenoort 1, J M Ghuysen 1
PMCID: PMC179500  PMID: 9324244

Abstract

Because the specificity profile of the membrane anchor-free G57-V577 penicillin-binding protein 3 (PBP3) of Escherichia coli for a large series of beta-lactam antibiotics is similar to that of the full-size membrane-bound PBP, the truncated PBP is expected to adopt the native folded conformation. The truncated PBP3 functions as a thiolesterase. In aqueous media and in the presence of millimolar concentrations of a properly structured amino compound, it catalyzes the aminolysis of the thiolester until completion, suggesting that the penicillin-binding module of PBP3 is designed to catalyze transpeptidation reactions. In contrast, the truncated PBP3 is devoid of glycan polymerization activity on the E. coli lipid II intermediate, suggesting that the non-penicillin-binding module of PBP3 is not a transglycosylase.

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Selected References

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