doi: 10.1093/oxfordjournals.jbchem.a130812.
Phosphorylation of D-glucosamine by rat liver glucokinase
- PMID: 1158856
- DOI: 10.1093/oxfordjournals.jbchem.a130812
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Phosphorylation of D-glucosamine by rat liver glucokinase
J Biochem.
1975 May.
Free article
Abstract
D-Glucosamine was found to be phosphorylated by a rat liver extract in the presence of a high concentration of glucose, which was formerly believed to be a strong competitive inhibitor of this reaction. Results suggested that glucosamine may be phosphorylated by high Km hexokinase, i.e. glucokinase [EC 2.7.1.2]. The enzyme involved was separated from specific N-acetyl-D-glucosamine kinase [EC 2.7.1.59]. The phosphorylation was not inhibited by a physiological level of glucose or glucose 6-phosphate, which strongly inhibited low Km hexokinase. The apparent Km of glucokinase for glucosamine was estimated as 8 mM, which is ten times that of low Km hexokinase.
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