抄録
The metabolism of levoglucosan (l, 6-anhydro-β-D-glucopyranose) in several microorganisms was studied. Although levoglucosan could be easily hydrolyzed to glucose with acid, all of the tested yeasts and fungi strains had no activity hydrolyzing it. On the other hand, the formation of glucose 6-phosphate from levoglucosan in the presence of Mg-ATP2- was observed in the reaction with the cell extracts of all levoglucosan-assimilating yeasts and fungi. The enzyme catalyzing this formation of glucose 6-phosphate was shown to be independent of the general hexokinases by an ion-exchange chromatography or poly aery lamide gel electrophoresis followed by staining of the activities. These data showed that levoglucosan would be directly phosphorylated to glucose 6-phosphate with a specific enzyme, levoglucosan kinase, and then metabolized through the general glycolytic pathway.
