Cooperative Effects of Light and Temperature on the Activity of Phosphoenolpyruvate Carboxylase from Amaranthus paniculatus L.
- 1 October 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 82 (2), 518-522
- https://doi.org/10.1104/pp.82.2.518
Abstract
The phosphoenolpyruvate carbocylase of Amaranthus paniculatus shows in vitro optimum affinity (S0.5) to phosphoenolpyruvate at a relatively high temperature (about 35.degree.C); even in the presence of activators, it functions efficiently only above 25 to 27.degree.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.This publication has 11 references indexed in Scilit:
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