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- W2073294431 abstract "Fructose is converted to glucose in a dialyzed liver homogenate fortified with an oxidizable substrate, Mg++ and a catalytic amount of ATP. In the presence of fluoride, the conversion of fructose to glucose is inhibited, and an acid-labile phosphate ester accumulates. Isolation and characterization by its strong negative specific rotation, hydrolysis constant in acid, and liberation of inorganic phosphate on forming the osazone, identified this ester as funcoose-1-phosphate. Another acid-labile phosphate ester which accumulated even in the absence of a phosphate acceptor was isolated as the crystalline sodium salt and identified as inorganic pyrophosphate.A protein fraction precipitated from liver extract between 0.45 and 0.55 saturation with ammonium sulfate catalyzed the conversion of fructose-1-phosphate to hexose-6-phosphate. This mutase reaction was accelerated by Mg++ ions and inhibited by fluoride. In liver homogenate, in the absence of fluoride, the mutase reaction is followed by dephosphorylation of hexose-6-phosphate to free glucose and inorganic phosphate. These three enzymatic reactions explain the mechanism of conversion of fructose to glucose in the liver.The formation of fructose-1-phosphate by liver fructokinase is not inhibited by glucose, in contrast to the strong inhibition glucose exerts on the phosphorylation of fructose by yeast and brain hexokinase. Fructose utilization in the liver is thus independent of glucose utilization, the latter being catalyzed by a separate enzyme. The liver fructokinase is much more active in an aerobic system with catalytic amounts of ATP than in an anaerobic system with an excess of ATP.A summary of the enzymatic reactions concerned with the metabolism of fructose in various tissues is presented." @default.
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- W2073294431 date "1951-01-01" @default.
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- W2073294431 title "The metabolism of fructose in liver. Isolation of fructose-1-phosphate and inorganic pyrophosphate" @default.
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- W2073294431 doi "https://doi.org/10.1016/0006-3002(51)90032-7" @default.
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