A suicide-substrate mechanism for hydrolysis of beta-lactams by an anti-idiotypic catalytic antibody.
The catalytic mechanism of an anti-idiotypic antibody, 9G4H9, displaying a beta-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.
Génie Enzymatique et Cellulaire, UMR 6022 CNRS, Université de Technologie de Compiègne, P.O. Box 20529, 60205 Cedex, Compiegne, France.
S
S
Lefevre
H
H
Debat
D
D
Thomas
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A
Friboulet
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B
Avalle
D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000378:metabolism*; D017151:Antibodies, Catalytic / Q000737:chemistry / Q000378:metabolism*; D000911:Antibodies, Monoclonal / Q000378:metabolism; D015153:Blotting, Western; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D051379:Mice; D010406:Penicillins / Q000494:pharmacology; D013379:Substrate Specificity; D047090:beta-Lactams / Q000378:metabolism*
D000888:Antibodies, Anti-Idiotypic; D017151:Antibodies, Catalytic; D000911:Antibodies, Monoclonal; D010406:Penicillins; D047090:beta-Lactams