Unknown

Dataset Information

0

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


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.

SUBMITTER: Murphy BP 

PROVIDER: S-EPMC1135462 | biostudies-other | 1988 Dec

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC4204886 | biostudies-literature
| S-EPMC3684201 | biostudies-literature
| S-EPMC3985439 | biostudies-literature
| S-EPMC1131754 | biostudies-other
| S-EPMC1151417 | biostudies-other
| S-EPMC1135750 | biostudies-other
| S-EPMC4946933 | biostudies-literature
| S-EPMC4498786 | biostudies-literature
| S-EPMC6767355 | biostudies-literature
| S-EPMC7863881 | biostudies-literature