Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.
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.
Prosperi-Meys
C
C
Centre d'Ingénierie des Protéines (B6), Université de Liège, Belgium. christelle.prosperi@ulg.ac.be
Llabres
G
G
de Seny
D
D
Soto
R P
RP
Valladares
M H
MH
Laraki
N
N
Frere
J M
JM
Galleni
M
M
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*