Abstract
A new enzyme named levoglucosan kinase, which catalyzes the direct phosphorylation of levoglucosan (1,6-anhydro-β-d-glucopyranose) to glucose 6-phosphate in the presence of Mg-ATP2-, was purified from the crude extract of a yeast, Sporobolomyces salmonicolor, and characterized. This enzyme was induced only by levoglucosan and it had such a strict substrate specificity that mannosan (1,6-anhydro-β-d-mannopyranose) alone other than levoglucosan was slightly phosphorylated. Only gentiobiose, among various sugars, showed a weak noncompetitive inhibition for the phosphorylation of levoglucosan. The Km for levoglucosan was very high, 85 mm, but that for ATP was 0.19 mm, as high as in general hexokinases. This is the first enzyme to act on an anhydro-sugar like levoglucosan in vivo.
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