The importance of the negative charge of β‐lactam compounds for the inactivation of the active‐site serine DD‐peptidase of Streptomyces R61

FEBS Letters

Ghuysen, Jean-Marie¹  Frère, Jean-Marie¹  Varetto, Louis¹ 

[1] Service de Microbiologie, Université de Liège, Institut de Chimie, B6, Sart Tilman, B-4000 Liège, Belgium

关键词: β-Lactam;    pH dependence;    Enzyme inactivation;    Deacetyl-cephalosporin C;    DD-peptidase;   

DOI  :  10.1016/0014-5793(87)81161-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction between the Streptomyces R61 penicillin-sensitive DD-peptidase and deacetyl-cephalosporin C or its lactone derivative has been studied at different pH values. The results show the importance of an enzyme group of pK ≌ 9 which might form an ion pair with the free carboxylate of the former compound. This electrostatic interaction is shown to contribute to the formation of the first, non-covalent enzyme-inactivator complex by a factor of at least 50.

【 授权许可】

Unknown