ORBi: Frère Jean-Marie - Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models

Reference : Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from ...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Microbiology Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/83081

Title :	Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics. A choice of models
Language :	English
Author, co-author :	Frère, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
	Iwatsubo, Motohiro [Centre National de la Recherche Scientifique - CNRS > Centre de Génetique Moléculaire > > >]
Publication date :	15-Sep-1975
Journal title :	European Journal of Biochemistry
Publisher :	Blackwell Science
Volume :	57
Issue/season :	2
Pages :	343-351
Audience :	International
ISSN :	0014-2956
e-ISSN :	1432-1033
City :	Oxford
Country :	United Kingdom
Keywords :	[en] acyltransferases/metabolism ; ampicillin/metabolism ; binding sites ; carbenicillin/metabolism ; carboxypeptidases/metabolism ; kinetics ; mathematics ; penicillin g/metabolism ; penicillins/metabolism ; peptidyl transferases/metabolism ; protein binding ; streptomyces/*enzymology
Abstract :	[en] The simplest model for the interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and beta-lactam antibiotics involves the three following steps: (a) the formation of a reversible equimolar enzyme - antibiotic complex; (b) the irreversible transformation of this complex into a modified enzyme - antibiotic complex; and (c) the breakdown of this latter complex and the concomitant release of a regenerated enzyme and a modified antibiotic molecule. The dissociation constant for step 1 and the rate constants for steps 2 and 3 were measured with various beta-lactam antibiotics. With antibiotic such as benzylpenicillin, which behaves as a good 'substrate', steps 1 and 2 occur at enzymic velocities, whereas step 3 occurs at a very low velocity and hence is responsible for the low efficiency of the overall process.
Funders :	Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Fondamentale Collective
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/83081

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