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Plant Physiology 82:518-522 (1986)
© 1986 American Society of Plant Biologists

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Cooperative Effects of Light and Temperature on the Activity of Phosphoenolpyruvate Carboxylase from Amaranthus paniculatus L. 1

Eleni Selinioti2, Yiannis Manetas and Nikos A. Gavalas

Department of Biology, University of Patras, Patras, Greece, Laboratory of Plant Physiology, University of Patras, Patras, Greece

The phosphoenolpyruvate carboxylase of Amaranthus paniculatus shows in vitro optimum affinity (S0.5) to phosphoenolpyruvate at a relatively high temperature (about 35°C); even in the presence of activators, it functions efficiently only above 25 to 27°C. At lower temperatures, a steep increase of activity with temperature is observed, due to the high activation energy for the catalyzed reaction. The same behavior in vivo could amplify the photoactivation of the enzyme to a large extent, since the night/day transition is soon followed by a considerable rise in leaf temperature.

2 From her Doctoral Thesis.

1 Supported by the State Scholarship Foundation (Greece) through a scholarship to E. S. The final experimental stage was also supported financially through a Grant from the Ministry of Research and Technology.




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B. Chinthapalli, J. Murmu, and A. S. Raghavendra
Dramatic difference in the responses of phosphoenolpyruvate carboxylase to temperature in leaves of C3 and C4 plants
J. Exp. Bot., February 1, 2003; 54(383): 707 - 714.
[Abstract] [Full Text] [PDF]


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Copyright © 1986 by the American Society of Plant Biologists