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-P(2)ase) were identified in leaves of corn (Zea mays), a C(4) plant. Fru-6-P,2K and Fru-2,6-P(2)ase 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 C(3) 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-P(2)ase was inhibited by its products, fructose-6-phosphate and Pi. However, unlike its spinach equivalent, corn Fru-2,6-P(2)ase was also inhibited by 3-phosphoglycerate and, less effectively, by dihydroxyacetone phosphate. The C(4) Fru-6-P,2K and Fru-2,6-P(2)ase were also quite sensitive to inhibition by phosphoenolpyruvate, and each enzyme was also selectively inhibited by certain other metabolites.
No takes yet. Share an insight, caveat, or question.
Soll et al. (1985) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: