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[The role of a cosubstrate in the kinetic mechanism of action of mollusk thiaminase I].

Mechanisms of interaction between thiaminase I and cosubstrate were studied using thiazole-2-14C-thiamine and 14C-nicotinic acid. The dissociation constant of nicotinic acid in the presence of the enzyme was of an order of 1 x 10(-6) M. A mechanism of the prestationary phase of a thiaminase reaction at -10 degrees was studied. The low temperature step, which demonstrated specific characteristics, was involved in analytic estimation of total thiamine concentration in vitro. Native thiaminase I from the bivalve mollusca Anodonta cygnea proved to be a holoenzyme.