Phosphoenolpyruvate-dependent phosphorylation of alpha-methylglucoside in Streptococcus sanguis ATCC 10556.

Spontaneous mutants defective in some undefined membrane components of the phosphoenolpyruvate:glucose phosphotransferase system were isolated by plating cells of Streptococcus sanguis ATCC 10556 onto an agar containing lactose and 10 mM 2-deoxyglucose. Toluenized cells of these mutants were defective in their ability to catalyse the phosphoenolpyruvate-dependent phosphorylation of 2-deoxyglucose but were still able to phosphorylate alpha-methylglucoside. The phosphorylation of alpha-methylglucoside was essentially dependent on phosphoenolpyruvate and required the presence of both soluble and membrane components. It was concluded that S. sanguis possessed two different phosphoenolpyruvate:glucose phosphotransferase systems.