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Purification and Characterization of Phosphoenolpyruvate Carboxylase from Maize Leaves ¹

^a Department of Agricultural Chemistry, School of Agriculture, Shizuoka University, Ohya 836, Shizuoka 422, Japan

Phosphoenolpyruvate carboxylase has been purified to homogeneity from maize (Zea mays L. var. Golden Cross Bantam T51) leaves. The ratio of specific activities in crude extracts and the purified enzyme suggests that the enzyme is a major soluble protein in the tissue. The enzyme has a sedimentation coefficient (s_20,w) of 12.3S and a molecular weight, determined by sedimentation equilibrium, of 400,000 daltons. Dissociation of the enzyme and electrophoresis on dodecyl sulfate polyacrylamide gels yields a single stained band which corresponds to a subunit weight of 99,000 daltons. Thus it appears that the native enzyme is composed of four identical or similar polypeptide chains.

The enzyme yields cooperative rate-concentration plots (Hill number of 2) with phosphoenolpyruvate as the variable substrate at pH 7. This cooperativity disappears in the presence of an activator, glucose-6-P, or by raising the pH of the assay mixture to 8. Glycerol (20%, v/v) exerts a similar effect. The enzyme is also activated in the presence of glycine which causes an increase in V_max without significant effect on the apparent Km for phosphoenolpyruvate and Hill number. The apparent Km for HCO₃^– is 0.02 mM, and the activation constant for Mg²⁺ is 1.54 mM at pH 7. There is an abrupt discontinuity in Arrhenius plots and an associated increase in activation energy below 10.8 C.

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