Abstract
Properties of phosphatase having specific activity for thiamine diphosphate and thiamine monophosphate were studied. When compared with p-nitrophenylphosphatase of L.fermenti, this phosphatase activity was inhibited by Mg^<2+> and Na_2MoO_4,while the p-nitrophosphatase was activated by Mg^<2+> and not affected by Na_2MoO_4. This enzyme activity was not affected by other phosphate compounds at all. When L.fermenti cells were cultivated with thiamine, the enzyme activity was decreased with increasing amounts of thiamine added to the medium.