1983
DOI: 10.1104/pp.73.1.188
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Fructose 2,6-Bisphosphate and the Regulation of Pyrophosphate-Dependent Phosphofructokinase Activity in Germinating Pea Seeds

Abstract: The activity of pyrophosphate:D-fructose-6-phosphate-1-phosphotransferase (EC 2.7

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Cited by 37 publications
(35 citation statements)
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“…Other sources of PPi production are less well established. 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).…”
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confidence: 99%
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“…Other sources of PPi production are less well established. 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).…”
mentioning
confidence: 99%
“…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).…”
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“…PFP activity has been found in many plantsZ~6, 13,14) and the enzymes from K. MIYATAKE, T. ENOMOTO and S. KITAOKA The activity was assayed in the presence (0) and absence of 1JiM Fru-2,6-P2 (e). Fru-6-P was varied against a constant concentration of pyrophosphate (1 mM).…”
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confidence: 99%