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. 1986 Oct;168(1):199–206. doi: 10.1128/jb.168.1.199-206.1986

Activity of penicillin-binding protein 3 from Escherichia coli.

A G Pisabarro, R Prats, D Váquez, A Rodríguez-Tébar
PMCID: PMC213438  PMID: 3531167

Abstract

The activity of penicillin-binding protein 3 of Escherichia coli has been studied both in vivo and in ether-permeabilized cells. The peptidoglycan transpeptidase activity of penicillin-binding protein 3 appears to use either nascent or exogenously added UDP-N-acetylmuramyl tripeptide-derived substrates as acceptors. By means of a defilamentation system which elicited the activity of penicillin-binding protein 3 in vivo, the structure of peptidoglycan made by this enzyme has been elucidated. This peptidoglycan, very probably of septal location, contained increased amounts of cross-linked peptidoglycan as well as a higher ratio of tripeptide-containing cross-linked subunits.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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