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Plasma Membrane Adenosine Triphosphatase of Oat Roots

Activation and Inhibition by Mg²⁺ and ATP ¹

^a Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907

ATPase activity of plasma membrane vesicles isolated from oat (Avena sativa L. cv. Goodfield) roots was examined in the presence of various concentrations of MgCl₂ and ATP. A Mg²⁺: ATP ratio of about 1 was required for maximal activity regardless of the concentrations used; the optimum concentration for both Mg²⁺ and ATP was 9 mM. Based on the ATPase activity at different concentrations of complexed Mg·ATP and free ATP, it is concluded that Mg·ATP is the true substrate of this enzyme.

Under certain experimental conditions, high concentrations of MgCl₂ and ATP inhibited the plasma membrane ATPase. On the basis of the relative amounts of free and complexed ATP and Mg²⁺, it was found that the different moieties caused different amounts of inhibition. Free ATP inhibited the ATPase at concentrations in excess of 2 mM. Mg·ATP concentrations above 11 mM inhibited the enzyme. Free Mg²⁺ caused only a slight inhibition of the ATPase.

The Km for Mg·ATP was found to vary from 0.64 to 1.24 mM depending on the experimental conditions. This variation is thought to be due to variable amounts of Mg·ATP, which serves as an inhibitor as well as the substrate, and free ATP, which also inhibits the enzyme.