Interaction between class B β‐lactamases and suicide substrates of active‐site serine β‐lactamases

FEBS Letters

Laraki, Netza²  Paul Soto, Raquel³  Prosperi-Meys, Christelle²  Hernandez Valladares, Maria²  Galleni, Moreno²  de Seny, Dominique²  Llabres, Gabriel¹  Frere, Jean-Marie² 

[1] Institut de Physique (B5), Université de Liège, Sart-Tilman, B-4000 Liège, Belgium;Centre d'Ingénierie des Protéines (B6), Université de Liège, Sart-Tilman, B-4000 Liège, Belgium;Fachrichtung 12.4 Biochemie, Universität des Saarlandes, Saarbrücken 6600, Germany

关键词: Metallo-β-lactamase;    Clavulanic acid;    Sulbactam;    Tazobactam;    6-β-Iodopenicillanic acid;   

DOI  :  10.1016/S0014-5793(98)01689-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The most widely used inactivators of active-site serine β-lactamases behave as substrates of four class B metallo-β-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the α and β isomers of 6-iodopenicillanic acid shows that there is no general preference for the α isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.

【 授权许可】

Unknown