Abstract
In plants that show Crassulacean acid metabolism, phosphoenolpyruvate carboxylase catalyses the key step of CO 2 fixation at night. We show here that the properties of this enzyme from Bryophyllum fedtschenkoi undergo marked changes between night and day; the night form is much less sensitive to feedback inhibition by malate than is the day form. Incubation of leaves with 32P i followed by extraction and immunoprecipitation of phosphoenolpyruvate carboxylase showed that only the night form contained 32P. This suggests that the activity of the enzyme is controlled by a covalent modification mechanism.
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