The regulation of phosphoenolpyruvate carboxylase in CAM plants

Nimmo, H. G. (2000) The regulation of phosphoenolpyruvate carboxylase in CAM plants. Trends in Plant Science, 5(2), pp. 75-80. (doi: 10.1016/S1360-1385(99)01543-5) (PMID:10664617)

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Abstract

Phosphoenolpyruvate carboxylase catalyses the primary assimilation of CO2 in Crassulacean acid metabolism plants. It is activated by phosphorylation, and this plays a major role in setting the day–night pattern of metabolism in these plants. The key factor that controls the phosphorylation state of phosphoenolpyruvate carboxylase is the activity of phosphoenolpyruvate carboxylase kinase. Recent work on Crassulacean acid metabolism plants has established this enzyme as a novel protein kinase and has provided new insights into the regulation of protein phosphorylation. Phosphoenolpyruvate carboxylase kinase is controlled by synthesis and degradation in response to a circadian oscillator. The circadian control of phosphoenolpyruvate carboxylase kinase can be overridden by changes in metabolite levels. The primary effect of the circadian oscillator in this system may be at the level of the tonoplast, and changes in kinase expression may be secondary to circadian changes in the concentration of a metabolite, perhaps cytosolic malate.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Nimmo, H. G.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Trends in Plant Science
Publisher:Elsevier Science
ISSN:1360-1385
ISSN (Online):1878-4372
Published Online:15 February 2000

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