Interaction of clavulanate with class C β‐lactamases

FEBS Letters

Monnaie, Didier¹  Frere, Jean-Marie¹ 

[1] Centre d'Ingénierie des Protéines and Laboratoire d'enzymologie, Université de Liège, B6 Sart-Tilman, B4000 Liège, Belgium

关键词: β-Lactamase;    Clavulanic acid;    AmpC;    Enterobacter cloacae 908R;    Serratia marcescens;    Escherichia coli K12;   

DOI  :  10.1016/0014-5793(93)80692-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interactions between clavulanate and three class C enzymes have been studied in detail. In all cases, the reactions followed branched pathways where 25–150 turnovers occurred before inactivation was completed. Reactivation rates were quite low. The poor efficiency of clavulanate as a class C inactivator appeared to rest upon a very slow acylation of the protein, and of a relatively high turnover rate.

【 授权许可】

Unknown