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- W2279429215 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." @default.
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- W2279429215 date "1988-12-01" @default.
- W2279429215 modified "2023-10-18" @default.
- W2279429215 title "Evidence for an oxyanion hole in serine <i>β</i>-lactamases and <scp>dd</scp>-peptidases" @default.
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- W2279429215 doi "https://doi.org/10.1042/bj2560669" @default.
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