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Volume 131, Issue 10

Inhibition and Inactivation of Glucose-phosphorylating Enzymes from Saccharomyces cerevisiae by D-Xylose Free

Abstract

Summary: Three glucose-phosphorylating enzymes were separated from cell-free extracts of by hydroxylapatite chromatography. Variations in the amounts of these enzymes in cells growing on glucose and on ethanol showed that hexokinase PI was a constitutive enzyme, whereas synthesis of hexokinase PII and glucokinase were regulated by the carbon source used. Glucokinase proved to be a glucomannokinase with values of 0.04 m for both glucose and mannose. D-Xylose produced an irreversible inactivation of the three glucose-phosphorylating enzymes depending on the presence or absence of ATP. Hexokinase PI inactivation required ATP, while hexokinase PII was inactivated by D-xylose without ATP in the reaction mixture. Glucokinase was protected by ATP from this inactivation. D-Xylose acted as a competitive inhibitor of hexokinase PI and glucokinase and as a non-competitive inhibitor of hexokinase PII.

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© Society for General Microbiology 1985
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1985-10-01
2024-04-19
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Inhibition and Inactivation of Glucose-phosphorylating Enzymes from Saccharomyces cerevisiae by D-Xylose
Microbiology 131, 2705 (1985); https://doi.org/10.1099/00221287-131-10-2705
/content/journal/micro/10.1099/00221287-131-10-2705
/content/journal/micro/10.1099/00221287-131-10-2705
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