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  • Title: Inactivation of the RTEM beta-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme.
    Author: Fisher J, Charnas RL, Bradley SM, Knowles JR.
    Journal: Biochemistry; 1981 May 12; 20(10):2726-31. PubMed ID: 7018564.
    Abstract:
    The characteristics of the reaction of a number of mechanism-based inactivators of the RTEM beta-lactamase have suggested that a common mechanistic pathway may be followed by many of these compounds. These ideas have been tested by the synthesis and evaluation of some penam sulfones as beta-lactamase inactivators. The sulfones of poor beta-lactamase substrates are, as predicted, potent inactivators of the enzyme. A unique serin residue (Ser-70) is labeled by quinacillin sulfone, and it is likely that this serine acts nucleophilically in the normal hydrolytic reaction of the beta-lactamase to form an acyl-enzyme intermediate.
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