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Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases
1Department of Chemistry, Wesleyan University, Middletown, CT 06457.
The Biochemical Journal
|December 1, 1988
Abstract:
A thionocephalosporin is shown to be a much poorer substrate of representative serine beta-lactamases of class A (RTEM-2) and class C (Enterobacter cloacae P99) and a much poorer inhibitor of the Streptomyces R61 DD-peptidase than is the analogous oxo beta-lactam. These results provide kinetic evidence for the existence of a catalytic oxyanion hole in these enzymes.