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Plant Physiology 84:58-60 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Anapleurotic CO2 Fixation by Phosphoenolpyruvate Carboxylase in C3 Plants 1

Eva Melzer and Marion H. O'Leary

Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706

The role of phosphoenolpyruvate carboxylase in photosynthesis in the C3 plant Nicotiana tabacum has been probed by measurement of the 13C content of various materials. Whole leaf and purified ribulose bisphosphate carboxylase are within the range expected for C3 plants. Aspartic acid purified following acid hydrolysis of this ribulose bisphosphate carboxylase is enriched in 13C compared to whole protein. Carbons 1-3 of this aspartic acid are in the normal C3 range, but carbon-4 (obtained by treatment of the aspartic acid with aspartate {beta}-decarboxylase) has an isotopic composition in the range expected for products of C4 photosynthesis (–5{per thousand}), and it appears that more than half of the aspartic acid is synthesized by phosphoenolpyruvate carboxylase using atmospheric CO2/HCO3–. Thus, a primary role of phosphoenolpyruvate carboxylase in C3 plants appears to be the anapleurotic synthesis of four-carbon acids.

1 Supported by contract DE-ACO2-83ER13076 and grant DE-FGO2-86ER13534 from the United States Department of Energy. Purchase of the mass spectrometer was supported by a grant from the National Science Foundation. E. M. was supported by a fellowship from Deutsche Forschungsgemeinschaft.




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