Structure-function analysis with a series of N-sulfonyloxy beta-lactam mole
cules as inhibitors of beta-lactamases is reported. The best of these compo
unds acylate the active site of the class A TEM-1 beta-lactamase from Esche
richia coli rapidly, and resist deacylation. Whereas acylation of the activ
e site of the class C beta-lactamase from Enterobacter cloacae was not seen
, these compounds function as competitive inhibitors of this enzyme. (C) 20
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