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Control of Photosynthetic Sucrose Synthesis by Fructose 2,6-Bisphosphate ¹

III. Properties of the Cytosolic Fructose 1,6-Bisphosphatase

Lehrstuhl für Biochemie der Pflanze, Universität Göttingen, Untere Karspüle 2, 3400 Göttingen, Federal Republic of Germany

The cytosolic fructose 1,6-bisphosphatase from spinach (Spinacia oleracea U.S. hybrid 424) leaves has been partially purified and its response to fructose 2,6-bisphosphate, AMP, and fructose 1,6-bisphosphate studied, using concentrations present in the cytosol during photosynthesis. In the presence of fructose 2,6-bisphosphate, the substrate saturation kinetics for fructose 1,6-bisphosphate are sigmoidal, with half-maximal activity being attained in 0.1 to 1 millimolar concentration range. The inhibition is enhanced by AMP. Using these results, and information published elsewhere on metabolite concentrations, it is discussed how fructose 1,6-bisphosphatase activity will vary in vivo in response to alterations in the availability of triose phosphate and AMP, and the accumulation of the product, fructose 6-phosphate.