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Reversible Inactivation of Rabbit Liver Fructose 1,6-Diphosphatase by Adenosine Triphosphate and Adenosine Diphosphate

From the ¹ From the Department of Microbiology, St. Louis University School of Medicine, St. Louis, Missouri 63104, and the Department of Biochemistry, Albany Medical College, Albany, New York 12208

ATP, ADP, and other nucleoside pyrophosphates converted homogeneous rabbit liver fructose 1,6-diphosphatase into a conformer with low catalytic activity, and altered the nature of the allosteric inhibition by AMP from sigmoidal to hyperbolic. This transition was both prevented and reversed by 3-phosphoglycerate or EDTA. Higher concentrations of inorganic phosphate and certain polycarboxylic acids and phosphate esters had similar effects. Two phosphonic acid analogues of ATP,ß,-methylene adenosine 5'-triphosphate and ,ß-methylene adenosine 5'-triphosphate, were found to inactivate the enzyme very specifically at much lower nucleotide concentrations. Mg²⁺ was required both for ATP inactivation to occur and for the prevention of this process by 3-phosphoglycerate. On the other hand, low concentrations of substrate markedly slowed down the interconversions in either direction.

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