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. 1985 Apr;77(4):999–1003. doi: 10.1104/pp.77.4.999

Enzyme Regulation in C4 Photosynthesis 1

Identification and Localization of Activities Catalyzing the Synthesis and Hydrolysis of Fructose-2,6-Bisphosphate in Corn Leaves

Jürgen Soll 1,2, Christiane Wötzel 1,3, Bob B Buchanan 1
PMCID: PMC1064647  PMID: 16664178

Abstract

Activities catalyzing the synthesis of fructose-2,6-bisphosphate (fructose-6-phosphate,2-kinase or Fru-6-P,2K) and its breakdown (fructose-2,6-bisphosphatase or Fru-2,6-P2ase) were identified in leaves of corn (Zea mays), a C4 plant. Fru-6-P,2K and Fru-2,6-P2ase were both localized mainly, if not entirely, in the leaf mesophyll cells. A partially purified preparation containing the two activities revealed that the kinase and phosphatase were regulated by metabolite effectors in a manner generally similar to their counterparts in C3 species. Thus, corn Fru-6-P,2K was activated by inorganic phosphate (Pi) and fructose-6-phosphate, and was inhibited by 3-phosphoglycerate and dihydroxyacetone phosphate. Fru-2,6-P2ase was inhibited by its products, fructose-6-phosphate and Pi. However, unlike its spinach equivalent, corn Fru-2,6-P2ase was also inhibited by 3-phosphoglycerate and, less effectively, by dihydroxyacetone phosphate. The C4 Fru-6-P,2K and Fru-2,6-P2ase were also quite sensitive to inhibition by phosphoenolpyruvate, and each enzyme was also selectively inhibited by certain other metabolites.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  2. Cséke C., Weeden N. F., Buchanan B. B., Uyeda K. A special fructose bisphosphate functions as a cytoplasmic regulatory metabolite in green leaves. Proc Natl Acad Sci U S A. 1982 Jul;79(14):4322–4326. doi: 10.1073/pnas.79.14.4322. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. El-Maghrabi M. R., Claus T. H., Pilkis J., Fox E., Pilkis S. J. Regulation of rat liver fructose 2,6-bisphosphatase. J Biol Chem. 1982 Jul 10;257(13):7603–7607. [PubMed] [Google Scholar]
  4. Jacquot J. P., Gadal P., Nishizawa A. N., Yee B. C., Crawford N. A., Buchanan B. B. Enzyme regulation in C4 photosynthesis: mechanism of activation of NADP-malate dehydrogenase by reduced thioredoxin. Arch Biochem Biophys. 1984 Jan;228(1):170–178. doi: 10.1016/0003-9861(84)90058-4. [DOI] [PubMed] [Google Scholar]
  5. Stitt M., Cseke C., Buchanan B. B. Regulation of fructose 2,6-bisphosphate concentration in spinach leaves. Eur J Biochem. 1984 Aug 15;143(1):89–93. doi: 10.1111/j.1432-1033.1984.tb08345.x. [DOI] [PubMed] [Google Scholar]
  6. Stitt M., Gerhardt R., Kürzel B., Heldt H. W. A role for fructose 2,6-bisphosphate in the regulation of sucrose synthesis in spinach leaves. Plant Physiol. 1983 Aug;72(4):1139–1141. doi: 10.1104/pp.72.4.1139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Stitt M., Wirtz W., Heldt H. W. Metabolite levels during induction in the chloroplast and extrachloroplast compartments of spinach protoplasts. Biochim Biophys Acta. 1980 Nov 5;593(1):85–102. doi: 10.1016/0005-2728(80)90010-9. [DOI] [PubMed] [Google Scholar]
  8. Usuda H., Edwards G. E. Localization of glycerate kinase and some enzymes for sucrose synthesis in c(3) and c(4) plants. Plant Physiol. 1980 May;65(5):1017–1022. doi: 10.1104/pp.65.5.1017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. van Schaftingen E., Davies D. R., Hers H. G. Fructose-2,6-bisphosphatase from rat liver. Eur J Biochem. 1982 May;124(1):143–149. doi: 10.1111/j.1432-1033.1982.tb05917.x. [DOI] [PubMed] [Google Scholar]

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