Activation of Higher Plant Phosphoenolpyruvate Carboxylases by Glucose-6-Phosphate

Abstract

Studies of the response of phosphoenolpyruvate carboxylase from C(3) (wheat [Triticum aestivum L.]), C(4) (maize [Zea mays L.]), and Crassulacean acid metabolism (CAM) (Crassula) leaves to the activator glucose-6-phosphate as a function of pH showed that the binding of the activator and the response path to activation were essentially identical for all three enzymes. The level of affinity for the activator differed, with the CAM enzyme having the highest affinity and the maize enzyme the lowest. The observed pK values suggest that histidine and cysteine groups may be involved in activation by glucose-6-phosphate. The presence of glucose-6-phosphate protected the enzyme against inactivation of the activation response by p-chloromercuribenzoate. The maximal activation response to glucose-6-phosphate showed differences among the three enzymes including different pH optima and different pH profiles. Here the maize leaf enzyme showed a potential response about twice as great as that of the C(3) and CAM enzymes.