Title: Activity of penicillin-binding protein 3 from Escherichia coli. | Journal: Journal of bacteriology. 1986 Oct;168(1):199-206 | Authors: Pisabarro AG, Prats R, Váquez D, Rodríguez-Tébar A. | 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. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/3531167 |
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