Reference : The Streptomyces DD-carboxypeptidase-transpeptidase system as a model for the study of p...

	Document type :	Scientific congresses and symposiums : Paper published in a book
	Discipline(s) :	Life sciences : Microbiology Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/91752

Title :	The Streptomyces DD-carboxypeptidase-transpeptidase system as a model for the study of penicillin action
Language :	English
Author, co-author :	Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie > > > >]
	Leyh-Bouille, Mélina [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie > > > >]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Dusart, Jean [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie > > > >]
	Perkins, Harold R. [National Institute for Medical Research - London > > > >]
	Nieto, Manuel [National Institute for Medical Research - London > > > >]
Publication date :	1972
Main document title :	Medicinal Chemistry : Special contributions - Milan 1972
Editor :	Pratesi, P.
Publisher :	Butterworths
Pages :	1-11
Audience :	International
City :	London
Event name :	3rd International Symposium on Medicinal Chemistry
Event date :	1972
Event place (city) :	Milan
Event country :	Italy
Keywords :	[en] penicillin
Abstract :	[en] A new model for the transpeptidation reaction involved in the biosynthesis of the bacterial wall peptidoglycan and for its inhibition by penicillin is proposed. This model is in open conflict with the hypotheses previously postulated. It rests upon the demonstration that 1) carboxypeptidase and transpep-tidase activities are performed by the same enzyme, 2) inhibition of both activities by penicillin is carried out in the absence of irreversible acylation of the protein, 3) the enzyme contains multiple sites some of which are involved in regulation, 4) penicillin does not act as a structural analogue of the donor peptide involved in transpeptidation but may act at the level of regulatory site(s).
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/91752

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