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Aspartic-acid synthesis in C3 plants
Authors:Eva Melzer  Marion H. O'Leary
Affiliation:(1) Departments of Chemistry and Biochemistry, University of Wisconsin-Madison, 53706 Madison, WI, USA;(2) Present address: Department of Biochemistry, University of Nebraska-Lincoln, 68583 Lincoln, NE, USA
Abstract:In a previous study (Melzer and O'Leary, 1987, Plant Physiol. 84, 58–60), we used isotopic methods to show that a substantial fraction of protein-bound aspartic acid in tobacco is derived from anaplerotic synthesis via phosphoenolpyruvate (PEP) carboxylase. Similar studies in soybean (Glycine max L.) and spinach (Spinacia oleracea L.) showed a similar pattern, and this pattern persists with age because of slow protein turnover. A more quantitative analysis indicates that about 40% of protein-bound aspartate is derived in this manner. Analyses of free aspartic and malic acids show that contribution of PEP carboxylase to the synthesis of these acids decreases with increasing age. The C4 plant Zea mays L. did not show this pattern.Abbreviations and Symbols RuBP ribulose bisphosphate - PEP phosphoenolpyruvate - OAA oxaloacetic acid - PGA 3-phosphoglyceric acid - delta13C carbon-13 - isotopic content [R(sample)/R(standard)-1] × 1000, where R = [13CO2]/[12CO2]This work was supported by contract DE-ACO2-83ER 13076 and grant DE-FGO2-86ER13534 from the U.S. Department of Energy. E. M. was supported by a fellowship from Deutsche Forschungsgemeinschaft. We are grateful to Isabel Treichel for assistance with isotopic analyses.
Keywords:Aspartic acid C3 plants (aspartic-acid synthesis)  Carbon-13  CO2 fixation  Phosphoenolpy ruvate carboxylase
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