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Plant and Cell Physiology, 1986, Vol. 27, No. 5 881-886
© 1986

Article

Enzymatic Properties of Phosphoenolpyruvate Carboxylase of Purified Chloroplasts from CAM-Performing Kalanchoe blossfeldiana Poelln. Plants

Véronique Adam and Pierre Rustin

Universitè Pierre el Marie Curie, Laboratoire de Biologie Végétale IV CNRS (UA 1180), 12, rue Cuvier, 75005 Paris, France

A phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.3 [EC] ) activity was associated with, the Percoll purified chloroplasts from Kalanchoe blossfeldiana leaves performing crassulacean acid metabolism (CAM) (plants grown under short-day conditions). Very little PEPC activity was detected in the chloroplasts when the plants were grown under long days, performing a C3-type photosynthetic metabolism. The PEPC activity measured in the chloroplasts from CAM-plants was very sensitive to such effectors as glucose-6-phosphate (G-6-P) and malate: the initial activity of PEPC in the presence of 1.2 mM PEP was 400% activated by 10 mM G-6-P and was 25% inhibited by 1 mM malate. These results show that the PEPC in the chloroplasts has the enzymatic characteristics described by Brulfert and Queiroz [(1982) Planta 154: 339] for PEPC extracted from CAM-performing K. blossfeldiana leaves.

(Received November 1, 1985; Accepted April 25, 1986)
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