Plant Physiology 51:448-453 (1973)
© 1973 American Society of Plant Biologists
Articles
Multiple Forms of Plant Phosphoenolpyruvate Carboxylase Associated with Different Metabolic Pathways 1
Irwin P. Tinga and
C. B. Osmondb
a Department of Biology, University of California, Riverside, California 92502,
b Department of Environmental Biology, Research School of Biological Sciences, A.N.U., Canberra, 2601, Australia
The physical and kinetic properties of multiple forms of phosphoenolpyruvate carboxylase were studied in leaves of C4 and C3 species, their F1 and F3 hybrids, in greening maize leaves, in Crassulacean acid metabolism plants, and in nongreen root tissues. Four different forms are suggested: a C4 photosynthetic phosphoenolpyruvate carboxylase with high Km for phosphoenolpyruvate ( 0.59 mM), Km Mg ( 0.5 mM), and Vmax ( 29 micromoles per minute per milligram of chlorophyll); a C3 photosynthetic phosphoenolpyruvate carboxylase with low Km for phosphoenolpyruvate ( 0.14 mM), Km for Mg ( 0.097 mM), and Vmax (1.5); a Crassulacean acid metabolism type with low Km for phosphoenolpyruvate (0.14 mM), and high Vmax (14 micromoles per minute per milligram of chlorophyll); and a nongreen or nonautotrophic type with low Km for phosphoenolpyruvate, Km for Mg, and low Vmax. In closely related species or within species, the types can be differentiated by anion exchange column chromatography. Each of the four forms is associated with a different metabolic pathway: the phosphoenolpyruvate carboxylase of C4 species for malate generation as a photosynthetic intermediate, the phosphoenolpyruvate carboxylase of C3 species in malate generation as a photosynthetic product, the phosphoenolpyruvate carboxylase of Crassulacean acid metabolism species in malate generation as a CO2 donor for photosynthesis during the subsequent light period, and a nongreen or root type producing malate for ionic balance and reduced nicotinamide adenine dinucleotide phosphate generation. The data in this paper in conjunction with published information support the notion of different molecular forms of a protein functioning in different metabolic pathways which have common enzymic steps.
1 This work was supported in part by National Science Foundation Grant GB 25878 and an Australian National University Visiting Fellowship to Irwin P. Ting.
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