A Kinetic Study of the NAD^+-Xylitol-Dehydrogenase from the Yeast Pichia stipits

概要

論文の詳細を見る
At physiological pH values the thermodynamic equilibrium constant was determined to be 6,9.10^<-11>(mol/l). Product inhibition studies are reported which clearly show that the kinetic mechanism of the NAD^+-xilitol dehydrogenase is "Ordered-bi-bi". It can be seen from experimental results that a cosubstrate inhibition with a dead and EA_2-complex occurs at elevated NAD^+-concentrations. Simulations were carried out which indicate, that under intracellular conditions the NAD^+-xylitol dehydrogenase is regulated by the catabolic reduction charge and not by the total concentration of NAD^+ and NADH.
社団法人日本生物工学会の論文
1989-01-25