ORBi: Ayala Juan - Site-directed mutagenesis of penicillin-binding protein 3 of Escherichia coli: role of Val-545

Reference : Site-directed mutagenesis of penicillin-binding protein 3 of Escherichia coli: role of V...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/85137

Title :	Site-directed mutagenesis of penicillin-binding protein 3 of Escherichia coli: role of Val-545
Language :	English
Author, co-author :	Ayala, Juan [Universidad Autonoma - Madrid > Centro de Biologica Molecular > > >]
	Goffin, Colette [Université de Liège - ULg > > Centre d'ingénierie des protéines > >]
	Nguyen-Distèche, Martine [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > > Centre d'Ingénierie des Protéines > >]
Publication date :	15-Aug-1994
Journal title :	FEMS Microbiology Letters
Publisher :	Blackwell Publishing
Volume :	121
Issue/season :	2
Pages :	251-256
ISSN :	0378-1097
e-ISSN :	1574-6968
City :	Oxford
Country :	United Kingdom
Keywords :	[en] bacterial proteins ; base sequence ; carrier proteins/genetics ; dna, complementary ; escherichia coli/chemistry/genetics/growth & development ; escherichia coli proteins ; hexosyltransferases ; molecular sequence data ; muramoylpentapeptide carboxypeptidase/*genetics ; mutagenesis, site-directed ; penicillin-binding proteins ; peptidoglycan glycosyltransferase ; peptidyl transferases ; valine/genetics
Abstract :	[en] Val545 of the Escherichia coli penicillin-binding protein 3 is essential to the acyl transfer mechanism through which the active-site serine 307 is acylated by benzylpenicillin and cephalexin and to the mechanism through which the protein allows rapidly growing cells to divide.
Research units :	Centre d'Ingénierie des Protéines - CIP
Funders :	Fonds de la Recherche Scientifique Médicale - FRSM ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/85137
DOI :	10.1111/j.1574-6968.1994.tb07106.x

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