[en] soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 (*PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli (14)C(-)labeled lipid 11 precursor. As a DD-peptidase, it could hydrolyze thiolester substrates with efficiencies similar to those of other class A penicillin-binding proteins (PBPs) and bind beta-lactams, but with k(2)/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs.
Disciplines :
Microbiology
Author, co-author :
Duez, Colette ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Hallut, Séverine; Université de Liège - ULiège > CIP
Rhazi, Noureddine ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Amoroso, Ana Maria ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Bouillenne, Fabrice ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Coyette, Jacques ; Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Language :
English
Title :
The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class a penicillin-binding protein
Publication date :
July 2004
Journal title :
Journal of Bacteriology
ISSN :
0021-9193
eISSN :
1098-5530
Publisher :
Amer Soc Microbiology, Washington, United States - Washington
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
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