[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Prosperi, Christelle ; Université de Liège - ULiège > Département de physique > Département de physique
Llabres, Gabriel ; Université de Liège - ULiège > Département de physique > Département de physique
De Seny, Dominique ; Centre Hospitalier Universitaire de Liège - CHU > Rhumatologie
Soto, R. P.
Valladares, M. H.
Laraki, Nadine ; Université de Liège - ULiège > Intervention et gestion en activités physiques et sportives
Frère, Jean-Marie ; Université de Liège - ULiège > Département des sciences de la vie > Département des sciences de la vie
Galleni, Moreno ; Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques
Language :
English
Title :
Interaction between Class B Beta-Lactamases and Suicide Substrates of Active-Site Serine Beta-Lactamases
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