J Biochem. 1975 May;77(5):1117-21.

Phosphorylation of D-glucosamine by rat liver glucokinase.

Oguchi M, Miyatake Y, Ayabe J, Akamatsu N.

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.

PMID:: 1158856; [PubMed - indexed for MEDLINE]

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Studies on the metabolism of hexosamine. A kinase activity for D-glucosamine without inhibition by glucose in rat liver and its possible identity with glucokinase. [J Biochem. 1977]
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