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Effects of 1,5‐anhydro‐D‐fructose on selected glucose‐metabolizing enzymes
Author(s) -
Taguchi T.,
Haruna M.,
Okuda J.
Publication year - 1993
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1993.tb00272.x
Subject(s) - hexokinase , fructose , glucokinase , biochemistry , phosphorylation , enzyme , yeast , chemistry , glucose oxidase , oxidase test , stereochemistry , glycolysis
It was verified, by n.m.r. and fast‐atom‐bombardment‐m.s. studies, that the C‐2 position of 1,5‐anhydro‐D‐fructose, which was prepared by the reaction of immobilized glucose 2‐oxidase from Coriolus versicolor (with 1,5‐anhydro‐D‐glucitol), is hydrated to the acetal form in water. The effects of 1,5‐anhydro‐D‐fructose on several glucose‐metabolizing enzymes were compared with those of 1,5‐anhydro‐D‐glucitol. Glucose 1‐oxidase from Aspergillus niger was inhibited by 1,5‐anhydro‐D‐fructose (Ki 6.6 mM) more effectively than 1,5‐anhydro‐D‐glucitol (Ki 82.5 mM). Yeast and rat brain hexokinases phosphorylated 1,5‐anhydro‐D‐fructose (Km, yeast 2.3 mM: Km, rat 0.79 mM) and 1,5‐anhydro‐D‐glucitol (Km, yeast 3.9 mM; Km, rat 0.83 mM). The phosphorylated forms of these compounds inhibited D‐glucose phosphorylation by yeast hexokinase (Ki of phosphorylated 1,5‐anhydro‐D‐fructose 0.11 mM; Ki of phosphorylated 1,5‐anhydro‐D‐glucitol 0.38 mM) and rat brain hexokinase (Ki of phosphorylated 1,5‐anhydro‐D‐fructose 0.07 mM; Ki of phosphorylated 1,5‐anhydro‐D‐glucitol 0.04 mM). Glucokinase phosphorylated neither 1,5‐anhydro‐D‐fructose nor 1,5‐anhydro‐D‐glucitol, and the phosphorylation of D‐glucose by glucokinase was inhibited by them. Mutarotase was slightly inhibited by 1,5‐anhydro‐D‐fructose, as well as by 1,5‐anhydro‐D‐glucitol.