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.
Research Article| December 01 1988
Evidence for an oxyanion hole in serine β-lactamases and dd-peptidases
B P Murphy;
Biochem J (1988) 256 (2): 669–672.
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B P Murphy, R F Pratt; Evidence for an oxyanion hole in serine β-lactamases and dd-peptidases. Biochem J 1 December 1988; 256 (2): 669–672. doi: https://doi.org/10.1042/bj2560669
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