1. Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases
- Author
-
Christelle Prosperi-Meys, Dominique de Seny, Maria Hernandez Valladares, Jean-Marie Frère, Netza Laraki, Moreno Galleni, Raquel Paul Soto, and Gabriel Llabres
- Subjects
Imipenem ,Tazobactam ,Stereochemistry ,Biophysics ,Alpha (ethology) ,Penicillanic Acid ,Biochemistry ,Catalysis ,beta-Lactamases ,Substrate Specificity ,Serine ,Isomerism ,Structural Biology ,Genetics ,medicine ,Binding site ,Beta (finance) ,Molecular Biology ,Clavulanic Acid ,chemistry.chemical_classification ,6-β-Iodopenicillanic acid ,Binding Sites ,biology ,Active site ,Metallo-β-lactamase ,Cell Biology ,Orders of magnitude (mass) ,Enzyme ,chemistry ,Sulbactam ,biology.protein ,medicine.drug - Abstract
The most widely used inactivators of active-site serine beta-lactamases behave as substrates of four class B metallo-beta-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the alpha and beta isomers of 6-iodopenicillanic acid shows that there is no general preference for the alpha isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.
- Published
- 1999