Partial purification and properties of a mannofructokinase from Streptococcus mutans SL-1.

Fructokinase activity was demonstrated in seven strains of oral streptococci. The enzyme purified from Streptococcus mutans SL-1 was capable of phosphorylating both D-fructose and D-mmannose to their respective 6-phosphates. Phosphorylation of both fructose and mannose was dependent on adenosine 5'-triphosphate and a divalent metal ion. The molecular weight of the purified enzyme was estimated to be 49,000. The apparent Km of the enzyme for fructose was 0.63 mM. This enzyme also utilized mannose as a substrate, with an apparent Km for mannose of 0.37 mM. Since the activities of the enzyme toward mannose and fructose were not separated upon purification of the enzyme and since mannose was a competitive inhibitor of fructose phosphorylation, the purified kinase is a single enzyme, mannofructokinase, with dual specificity for both mannose and fructose. A role for this enzyme in carbohydrate metabolism in S. mutans is postulated.