Purification and characterization of the VanB ligase associated with type B vancomycin resistance in Enterococcus faecalis V583

FEBS Letters

Badet-Denisot, Marie-Ange¹  Courvalin, Patrice²  Evers, Stefan²  Badeta, Bernard¹  Meziane-Cherif, Djalal¹ 

[1]Groupe Biocatalyse & Régulation, Institut de Chimie des Substances Naturelles, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France

[2]Unité des Agents Antibactériens, CNRS EP J0058, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France

关键词: D-Ala: D-Ala ligase;    Glycopeptide;    Vancomycin;    Depsipeptide;    Peptidoglycan;    Enterococcus;   

DOI  :  10.1016/0014-5793(94)01096-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Acquired resistance to glycopeptides in enterococci is associated with the production of D-Alanine: D-Alanine ligase-related proteins. The VanA protein associated with high-level vancomycin and teicoplanin resistance (VanA phenotype) synthesizes a new peptidoglycan precursor, D-alanine-D-lactate, that has reduced glycopeptide affinity. Production of a similar protein, VanB, is induced in strains that display variable levels of vancomycin resistance but remain susceptible to teicoplanin (VanB phenotype). This paper describes the over-production, purification and characterization of VanB. Comparison of kinetic parameters of the two Van enzymes suggests that differences in catalytic efficiency could account, at least in part, for the various levels of vancomycin resistance.

【 授权许可】

Unknown