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  • Title: Activity of penicillin-binding protein 3 from Escherichia coli.
    Author: Pisabarro AG, Prats R, Váquez D, Rodríguez-Tébar A.
    Journal: J Bacteriol; 1986 Oct; 168(1):199-206. PubMed ID: 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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