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Volume 133, Issue 2

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

Abstract

The hexose-ATP-kinase of wild-type (CBS 819) is, like hexokinase PII of , associated with carbon catabolite repression and phosphorylates -glucose and -fructose. The kinase of repression-resistant (Dog) mutants phosphorylates -glucose, but not -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 mutant of the (hexokinase PII) gene of , all failed to resolve more than one hexose-ATP-kinase in Hence appears to have a single hexose-ATP-kinase, ∼ 72000, with two catalytic sites, analogous to the aspartate kinase/homoserine dehydrogenase of One site is hexokinase-like and associated with catabolite repression and the other is glucokinase-like. Values for apparent were 7·2 m--fructose and 0·55 m--glucose (hexokinase site) and 0·078 m--glucose (glucokinase site).

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© Society for General Microbiology 1987
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1987-02-01
2024-04-24
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An Unusual Hexose-ATP-Kinase with Two Catalytic Sites and a Role in Carbon Catabolite Repression in the Yeast Schwanniomyces occidentalis
Microbiology 133, 381 (1987); https://doi.org/10.1099/00221287-133-2-381
/content/journal/micro/10.1099/00221287-133-2-381
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