Unknown

Dataset Information

0

Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase.


ABSTRACT: 6,6-Dithiodinicotinate shows half-of-the-sites reactivity towards the six catalytic-site thiol groups of bovine liver UDP-glucose dehydrogenase. The reagent introduces three intrasubunit disulphide linkages between catalytic-site thiol groups and non-catalytic-site thiol groups and abrogates 60% of the catalytic activity of the hexameric enzyme; excess 2-mercaptoethanol rapidly restores full catalytic activity. These results show the half-of-the-sites behaviour of the enzyme with the reagent and the presence of a non-catalytic-site thiol group capable of forming a disulphide linkage with a catalytic-site thiol group on the same subunit without irreversible denaturation.

SUBMITTER: Franzen JS 

PROVIDER: S-EPMC1185826 | biostudies-other | 1978 Aug

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1168171 | biostudies-other
| S-EPMC1164038 | biostudies-other
| S-EPMC1174227 | biostudies-other
| S-EPMC4498474 | biostudies-literature
| S-EPMC1163415 | biostudies-other
| S-EPMC1177692 | biostudies-other
| S-EPMC1174165 | biostudies-other
| S-EPMC1174164 | biostudies-other
| S-EPMC3272127 | biostudies-literature
| S-EPMC1198339 | biostudies-other