A suicide‐substrate mechanism for hydrolysis of β‐lactams by an anti‐idiotypic catalytic antibody

FEBS Letters

Debat, Hélène¹  Lefevre, Séverine¹  Friboulet, Alain¹  Avalle, Bérangère¹  Thomas, Daniel¹ 

[1] Génie Enzymatique et Cellulaire, UMR 6022 CNRS, Université de Technologie de Compiègne, P.O. Box 20529, 60205 Compiegne Cedex, France

关键词: Suicide substrate;    β-Lactamase;    Anti-idiotypic antibody;    Catalytic antibody;    Abzyme;    PBS;    phosphate-buffered saline;    BCA;    bicinchoninic acid;    ELISA;    enzyme-linked immunosorbent assay;    ABTS;    azino-bis(ethylbenzthiazoline sulfonate);    TBS;    tris(hydroxymethyl)aminomethane-buffered saline;    PBP;    penicillin-binding protein;   

DOI  :  10.1016/S0014-5793(01)02075-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The catalytic mechanism of an anti-idiotypic antibody, 9G4H9, displaying a β-lactamase activity was investigated. Kinetics experiments suggest that some penicillinic derivatives behave both as substrates and inactivators. Biochemical and immunological experiments strongly indicate that ampicillin may be regarded as a suicide substrate for hydrolysis by 9G4H9. The anti-idiotypic network appears as a way to create enzyme mimics with modified catalytic activities.

【 授权许可】

Unknown