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. 1987 May;84(1):58-60.
doi: 10.1104/pp.84.1.58.

Anapleurotic CO(2) Fixation by Phosphoenolpyruvate Carboxylase in C(3) Plants

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Anapleurotic CO(2) Fixation by Phosphoenolpyruvate Carboxylase in C(3) Plants

E Melzer et al. Plant Physiol. 1987 May.

Abstract

The role of phosphoenolpyruvate carboxylase in photosynthesis in the C(3) plant Nicotiana tabacum has been probed by measurement of the (13)C content of various materials. Whole leaf and purified ribulose bisphosphate carboxylase are within the range expected for C(3) plants. Aspartic acid purified following acid hydrolysis of this ribulose bisphosphate carboxylase is enriched in (13)C compared to whole protein. Carbons 1-3 of this aspartic acid are in the normal C(3) 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 C(4) photosynthesis (-5 per thousand), and it appears that more than half of the aspartic acid is synthesized by phosphoenolpyruvate carboxylase using atmospheric CO(2)/HCO(3) (-). Thus, a primary role of phosphoenolpyruvate carboxylase in C(3) plants appears to be the anapleurotic synthesis of four-carbon acids.

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