Fructose 2,6-bisphosphate, a potent regulator of carbohydrate metabolism, inhibits trehalose phosphorylase from protist Euglena gracilis.
Partially purified trehalose phosphorylase (EC 2.4.1.64) from Euglena gracilis SM-ZK was inhibited by fructose 2,6-bisphosphate in both synthetic and degradative directions. Ki value for trehalose phosphorolysis was 1.2 microM and that for trehalose synthesis was 0.5 microM. Functions of fructose 2,6-bisphosphate in Euglena, particularly in the regulative mechanism of the two reserve carbohydrates, paramylon and trehalose, are discussed.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000818:Animals; D001667:Binding, Competitive; D005056:Euglena gracilis / Q000201:enzymology*; D005635:Fructosediphosphates / Q000494:pharmacology*; D005964:Glucosyltransferases / Q000037:antagonists & inhibitors*; D006598:Hexosediphosphates / Q000494:pharmacology*; D006600:Hexosephosphates / Q000494:pharmacology; D007700:Kinetics
D000227:Adenine Nucleotides; D005635:Fructosediphosphates; D006598:Hexosediphosphates; D006600:Hexosephosphates; C027652:fructose 2,6-diphosphate; D005964:Glucosyltransferases; C023181:alpha,alpha-trehalose phosphorylase