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Participation of the enzyme which provides the phosphorylation of thiamine to thiamindiphosphate (TDP) thiaminkinase (thiaminpyrophosphokinase, KF 2.7.6.2) of rat brain in the realization of thiamine action on the syntheses of acethylcholine (AC) was studied. The thiamine and its structure analogue, which differ the nature of the radicals in the 3-d and 5-e positions of the thiazollium cycle were used: 3-[(4-amino-2methylpyrimidinyl-5)methyl]-4-methylthiazolium chloride, 3-decyloxycarbonylmethyl-4-metyl-5-beta-hydrozyethylthiazolium chloride, 3-decyloxycarbonylmethyl-4-methylthiazolium chloride. All salts in the concentrations lower then Km render active influence on thiaminkinase. The analysis of data shows the presence of the regulation site on the enzyme distinguishing from the active enzyme centre and participating in the interaction with which the hydrophobic fragments of thiamine molecule participating. The comparative studies of thiamine and above mentioned derivatives influence on the inclusion of the labelled carbon with [2-(14)C] pyruvate in acethylcholine confirm an assumption about the key-role of the thiamine interaction with thiaminkinase (meaning its phosphorilation) regarding its action on the acethylcholine syntheses, and probably, on the function of the nervous cells as a whole.