“…Although PPi-PFK is a reversible enzyme in vitro and could participate in gluconeogenesis in tissues such as castor bean endosperm which undergo a rapid conversion of fat to sugar (6), data on fru 2,6-P2-induced aggregation of PPi-PFK (14,15) and the kinetic characteristics of PPi-PFK (2, 13-15) support a glycolytic function for the enzyme. Fru 2,6-P2 promotes the association of a large molecular form of PPi-PFK which favors the glycolytic over the gluconeogenic direction of enzymic activity (14,15), and fru 2,6-P2 stimulates the glycolytic direction of PPi-PFK at lower concentrations than the gluconeogenic direction (13)(14)(15). Several workers indicate that fru 2,6-P2 is present in plant tissues in significant amounts (5,10,12,13) and its concentration fluctuates depending on parameters such as physiological condition of the plant (5,12) or physical factors such as light (10).…”