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. 1988 Dec 1;256(2):669–672. doi: 10.1042/bj2560669

Evidence for an oxyanion hole in serine beta-lactamases and DD-peptidases.

B P Murphy 1, R F Pratt 1
PMCID: PMC1135462  PMID: 3066349

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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