Evidence for an oxyanion hole in serine β-lactamases and dd-peptidases
- 1 December 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 256 (2) , 669-672
- https://doi.org/10.1042/bj2560669
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.This publication has 24 references indexed in Scilit:
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