English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The hexose-ATP-kinase of wild-type Schwanniomyces occidentalis (CBS 819) is, like hexokinase PII of Saccharomyces cerevisiae, associated with carbon catabolite repression and phosphorylates D-glucose and D-fructose. The kinase of Schw. occidentalis repression-resistant (DogR) mutants phosphorylates D-glucose, but not D-fructose. Subjecting the wild-type enzyme to 45 °C for a few minutes appears to alter its activity, specificity and kinetic characteristics to that of the mutant enzyme. Fast protein liquid chromatography, with anion-exchange or gel-filtration columns, gel-electrophoresis, and DNA hybridization with the hexlr mutant of the HXK2 (hexokinase PII) gene of Sacch. cerevisiae, all failed to resolve more than one hexose-ATP-kinase in Schw. occidentalis. Hence Schw. occidentalis appears to have a single hexose-ATP-kinase, Mr ∼ 72000, with two catalytic sites, analogous to the aspartate kinase/homoserine dehydrogenase of Escherichia coli. One site is hexokinase-like and associated with catabolite repression and the other is glucokinase-like. Values for apparent Km were 7.2 mM-D-fructose and 0.55 mM-D-glucose (‘hexokinase’ site) and 0.078 mM-D-glucose (‘glucokinase’ site).

An Unusual Hexose-ATP-Kinase with Two Catalytic Sites and a Role in Carbon Catabolite Repression in the Yeast Schwanniomyces occidentalis