Answers are grounded in this paper and cite their sources.
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.
No takes yet. Share an insight, caveat, or question.
Murphy et al. (1988) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: