Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 100:382-387 (1992)
© 1992 American Society of Plant Biologists

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Metabolism and Enzymology

Inactivation of Maize Leaf Phosphoenolpyruvate Carboxylase by the Binding to Chloroplast Membranes 1

Min-Xian Wu2 and Randolph T. Wedding

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

Phosphoenolpyruvate carboxylase (PEPC) purified from maize (Zea mays L.) leaves associates with maize leaf chloroplast membrane in vitro. The binding of PEPC to the membrane results in enzyme inactivation. A protein isolated from a maize leaf chloroplast membrane preparation inactivated PEPC. Treatment with membrane preparation or with partially purified inactivating protein accelerates PEPC inactivation at low temperature (4°C). Interaction of PEPC with chloroplast membrane or inactivating protein may inactivate the enzyme by influencing dissociation of the enzyme active tetramer.

2 Permanent address: Institute of Plant Physiology, Academia Sinica, Shanghai, The People's Republic of China.

1 Supported in part by National Science Foundation grant No. DCB 88-12484.






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Copyright © 1992 by the American Society of Plant Biologists