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Journal of Bacteriology, July 2004, p. 4412-4416, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4412-4416.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The ponA Gene of Enterococcus faecalis JH2-2 Codes for a Low-Affinity Class A Penicillin-Binding Protein

Centre d'Ingénierie des Protéines, Institut de Chimie, B6, Université de Liège, B-4000 Sart Tilman, Belgium,¹ Laboratorio de Resistencia Bacteriana, Facultad de Farmacia y Bioquimica, Universidad de Buenos Aires, 1113 Buenos Aires, Argentina²

Received 27 December 2003/ Accepted 29 March 2004

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 ß-lactams, but with k₂/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs.

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