Modular Design of the Bi(Multi?)Functional Penicillin-Binding Proteins

  • Serge Englebert
  • Aboubaker El Kharroubi
  • Graziella Piras
  • Bernard Joris
  • Jacques Coyette
  • Martine Nguyen-Distèche
  • Jean-Marie Ghuysen
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 65)

Abstract

The penicilloyl serine transferases are proteins or protein domains that catalyse rupture of the β-lactam amide bond of penicillin and transfer of the penicilloyl moiety to an essential serine. The serine-ester-linked penicilloyl derivatives formed by reaction with the β-lactamases are hydrolytically labile. Those formed by reaction with the penicillin-binding proteins (PBPs) are hydrolytically inert. Penicilloylation of the essential serine of some PBPs produces a signal that is transmitted to the cytosol. Penicilloylation of other PBPs causes loss of a catalytic function related to wall peptidoglycan synthesis. For a recent review and list of references, see Ghuysen (1991).

Keywords

Terminal Domain Neisseria Gonorrhoeae Neisseria Meningitidis Diamino Acid Hydrophobic Cluster Analysis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Serge Englebert
    • 1
  • Aboubaker El Kharroubi
    • 1
  • Graziella Piras
    • 1
  • Bernard Joris
    • 1
  • Jacques Coyette
    • 1
  • Martine Nguyen-Distèche
    • 1
  • Jean-Marie Ghuysen
    • 1
  1. 1.Centre d’Ingénierie des ProtéinesUniversité de Liège, Institut de ChimieLiège 1Belgium

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