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The Cyanide Adduct of the Aldolase Dihydroxyacetone Phosphate Imine

From the ¹ From the Department of Neurology, Columbia University, College of Physicians and Surgeons, New York, New York 10032

Aldolase was slowly inhibited in the presence of dihydroxyacetone phosphate and hydrogen cyanide. Activity was recovered on removal of these reagents. Neither dihydroxyacetone phosphate or hydrogen cyanide separately nor dihydroxyacetone with cyanide inhibited aldolase. The formation of an inactive aminonitrile enzyme derivative by addition of cyanide to an enzyme-substrate imine (Schiff base) is postulated. The rate and equilibrium constants for inhibition were marginally lower for carboxypeptidase A-treated aldolase than for native aldolase.

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