Abstract
Historically seven Penicillin Binding Proteins (PBPs) have been recognised in Escherichia coli, though with recent work two more have been added. Two of the PBPs, PBP2 and PBP3 have distinct morphological roles (Spratt, 1983). PBP2 is involved in cell elongation and allows the rod shape to be maintained, while by contrast PBP3 is required for septum formation, and its inhibition leads to filamentation and lysis. Both these proteins have been demonstrated to have transpeptidase and associated transglycosylase activity (Ishino & Matsuhashi 1983. Ishino et al 1986).
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© 1993 Springer Science+Business Media New York
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Edwards, D.H., Donachie, W.D. (1993). Construction of a Triple Deletion of Penicillin-Binding Proteins 4, 5, and 6 in Escherichia coli . In: de Pedro, M.A., Höltje, JV., Löffelhardt, W. (eds) Bacterial Growth and Lysis. Federation of European Microbiological Societies Symposium Series, vol 65. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9359-8_44
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DOI: https://doi.org/10.1007/978-1-4757-9359-8_44
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