VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

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

   
Puzach S.S., Gorbach Z.V.
PubMed Id: 8511878
Year: 1993  Volume: 39  Issue: 2  Pages: 19-21
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.
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Puzach, S. S., Gorbach, Z. V. (1993). The role of a cosubstrate in the kinetic mechanism of action of mollusk thiaminase I. Voprosy Meditsinskoi Khimii, 39(2), 19-21.
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