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Plant Physiology 100:1366-1368 (1992)
© 1992 American Society of Plant Biologists

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Metabolism and Enzymology

Inactivation of Maize Phosphoenolpyruvate Carboxylase by Urea 1

Randolph T. Wedding, Paul Dole, Thierry P. Chardot and Min-Xian Wu

Department of Biochemistry, University of California, Riverside, California 92521

Phosphoenolpyruvate carboxylase purified from leaves of maize (Zea mays, L.) is sensitive to the presence of urea. Exposure to 2.5 M urea for 30 min completely inactivates the enzyme, whereas for a concentration of 1.5 M urea, about 1 h is required. Malate appears to have no effect on inactivation by urea of phosphoenolpyruvate carboxylase. However, the presence of 20 mM phosphoenolpyruvate or 20 mM glucose-6-phosphate prevents significant inactivation by 1.5 M urea for at least 1 h. The inactivation by urea is reversible by dilution. The inhibition by urea and the protective effects of phosphoenolpyruvate and glucose-6-phosphate are associated with changes in aggregation state.

1 Supported in part by grant DCB 88-12484 from the National Science Foundation.






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Copyright © 1992 by the American Society of Plant Biologists