The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class A penicillin-binding protein |
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| Authors: | Duez Colette Hallut Séverine Rhazi Noureddine Hubert Séverine Amoroso Ana Bouillenne Fabrice Piette André Coyette Jacques |
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| Institution: | Centre d'Ingénierie des Protéines, Institut de Chimie, B6, Université de Liege, B-4000 Sart Tilman, Belgium. jcoyette@ulg.ac.be |
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| Abstract: | A 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 14C-labeled lipid II 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 k2/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs. |
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