| Literature DB >> 15205448 |
Colette Duez1, Séverine Hallut, Noureddine Rhazi, Séverine Hubert, Ana Amoroso, Fabrice Bouillenne, André Piette, Jacques Coyette.
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.Entities:
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Year: 2004 PMID: 15205448 PMCID: PMC421628 DOI: 10.1128/JB.186.13.4412-4416.2004
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490