Interaction between class B β‐lactamases and suicide substrates of active‐site serine β‐lactamases

Abstract
The most widely used inactivators of active-site serine β-lactamases behave as substrates of four class B metallo-β-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the α and β isomers of 6-iodopenicillanic acid shows that there is no general preference for the α isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.