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 vol: 39  issue:2  pages: 19-21
Abstract: 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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Reference: Puzach S.S., Gorbach Z.V., The role of a cosubstrate in the kinetic mechanism of action of mollusk thiaminase I, Voprosy meditsinskoi khimii, 1993, vol: 39(2), 19-21.
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