Purification and Characterization of Acid Phosphodiesterases of Cultured Tobacco Cells

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Two acid phosphodiesterases (phosphoric diester hydrolase, E.C. 3.1.4) were purified to apparent homogeneity from cultured cells of Nicotiana tabacum var. Bright Yellow. These enzymes appeared to differ in some physicochemical properties but exhibited similar broad substrate specificities towards cyclic and p-nitrophenyl nucleotides, and bis-p-nitrophenyl phosphate. Of these compounds, the most active substrates were bis-p-nitrophenylphosphate and 2, 3-cyclic nucleotides. Both p-nitrophenyl 3- and 5-thyrnidylates were hydrolyzed at comparable rates, whereas the hydrolysis of 3, 5-cyclic AMP occurred preferentially at the 5-phosphodiester bond. A unique catalytic property of these acid phosphodiesterases was the ability to liberate inorganic phosphate from ATP, ADP and p-nitrophenyl phosphate. Ribonucleic acid, its breakdown products, and inorganic phosphate were found to be effective as inhibitors.
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