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  • Title: Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.
    Author: Prosperi-Meys C, Llabres G, de Seny D, Soto RP, Valladares MH, Laraki N, Frere JM, Galleni M.
    Journal: FEBS Lett; 1999 Jan 25; 443(2):109-11. PubMed ID: 9989585.
    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.
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