title: Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.
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.
authors.affiliation: Centre d'Ingénierie des Protéines (B6), Université de Liège, Belgium. christelle.prosperi@ulg.ac.be
authors.forename: C
authors.initials: C
authors.lastname: Prosperi-Meys
authors.forename: G
authors.initials: G
authors.lastname: Llabres
authors.forename: D
authors.initials: D
authors.lastname: de Seny
authors.forename: R P
authors.initials: RP
authors.lastname: Soto
authors.forename: M H
authors.initials: MH
authors.lastname: Valladares
authors.forename: N
authors.initials: N
authors.lastname: Laraki
authors.forename: J M
authors.initials: JM
authors.lastname: Frere
authors.forename: M
authors.initials: M
authors.lastname: Galleni
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D019818:Clavulanic Acid / Q000378:metabolism; D007536:Isomerism; D010397:Penicillanic Acid / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D013407:Sulbactam / Q000378:metabolism; D000078142:Tazobactam; D001618:beta-Lactamases / Q000378:metabolism*