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Control of CO2 fixation regulation of stromal fructose-1,6-bisphosphatase in spinach by pH and Mg2+ concentration

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Abstract

The effect of pH and of Mg2+ concentration on the light activated form of stromal fructose-1,6-bisphosphatase (FBPase) was studied using the enzyme rapidly extracted from illuminated spinach chloroplasts. The (fructose-1,6-bisphosphate4-)(Mg2+) complex has been identified as the substrate of the enzyme. Therefore, changes of pH and Mg2+ concentrations have an immediate effect on the activity of FBPase by shifting the pH and Mg2+ dependent equilibrium concentration of the substrate. In addition, changes of pH and Mg2+ concentration in the assay medium have a delayed effect on FBPase activity. A correlation of the activities observed using different pH and Mg2+ concentrations indicates, that the effect is not a consequence of the pH and Mg2+ concentration as such, but is caused by a shift in the equilibrium concentration of a hypothetical inhibitor fructose-1,6-bisphosphate3- (uncomplexed), resulting in a change of the activation state of the enzyme. The interplay between a rapid effect on the concentration of the substrate and a delayed effect on the activation state enables a rigid control of stromal FBPase by stromal Mg2+ concentrations and pH. Fructose-1,6-bisphosphatase is allosterically inhibited by fructose-6-phosphate in a sigmoidal fashion, allowing a fine control of the enzyme by its product.

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Abbreviations

Fru1,6 bis P:

fructose-1,6-bisphosphate

Fru6P:

fructose-6-phosphate

FBPase:

fructose-1,6-bisphosphatase

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Some of these results have been included in a preliminary report (Heldt et al. 1984)

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Gardemann, A., Schimkat, D. & Heldt, H.W. Control of CO2 fixation regulation of stromal fructose-1,6-bisphosphatase in spinach by pH and Mg2+ concentration. Planta 168, 536–545 (1986). https://doi.org/10.1007/BF00392274

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  • DOI: https://doi.org/10.1007/BF00392274

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