Involvement of the NH2- and COOH-Terminal ends of PBP3 of Escherichia coli on β-Lactam Binding, Membrane Localization, and Function of the Protein

  • Manuel J. Gómez
  • Lourdes R. Desviat
  • Rafael Merchante
  • Juan A. Ayala
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 65)

Abstract

PBP3 of Escherichia coli is a membrane protein that has an essential function at the time of septum formation. This protein is involved in the last steps of incorporation of precursors into the septal peptidoglycan layer. Both transglycosylase and transpeptidase activities have been predicted for the protein, although only the transpeptidase activity has been repeatedly proved by “in vitro” assays. The protein binds the β-lactam antibiotics due to the structural homology of these compounds with the natural substrate for the enzyme, and they remain covalently linked due to the cyclic nature of the lactam ring and the mechanism of reaction.

Keywords

Glycerol Agar Penicillin Fractionation Serine 

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Manuel J. Gómez
    • 1
  • Lourdes R. Desviat
    • 1
  • Rafael Merchante
    • 1
  • Juan A. Ayala
    • 1
  1. 1.Centro de Biología MolecularCSIC — UAMMadridSpain

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