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

The presence of glucokinase (ATP:D-glucose 6-phosphotransferase, EC 2.7.1.2) activity in seven strains of oral streptococci is demonstrated. The glucokinase purified from Streptococcus mutans SL-1 cells is shown to be a highly specific enzyme, phosphorylating only glucose (eight sugars tested). The enzyme is a true glucokinase: formation of the product, shown here to be glucose 6-phosphate, is dependent on the presence of glucose, ATP, divalent metal ion and enzyme. The Km for glucose is 1.40 mM, the pH optimum for the enzyme is a broad plateu from pH 7.1 to 9.5 and the molecular weight is estimated to be 40 000. The finding of a glucokinase in oral streptococci indicates the existence of an intracellular mechanism of glucose phosphorylation. The implications of this observation are discussed.