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6-phosphofructo-2-kinase and D-fructose-2,6-bisphosphatase activities in mung bean seedlings



6-phosphofructo-2-kinase and D-fructose-2,6-bisphosphatase activities in mung bean seedlings



Biochimica et biophysica acta: general subjects 798(3): 317-324



6-Phosphofructo-2-kinase (ATP: D-fructose-6-phosphate-2-phosphotransferase) and D-fructose-2,6-bisphosphatase activities have been found in extracts prepared from etiolated mung bean seedlings. The activity of 6-phosphofructo-2-kinase exhibits a sigmoidal shape in response to changes in concentrations of both substrates, D-fructose 6-phosphate and ATP (S0.5 values of 1.8 and 1.2 mM, respectively). Inorganic orthophosphate (Pi) has a strong stimulating effect on the 2-kinase activity (A0.5 at about 2 mM), moderately increasing the Vmax and modifying the response into hyperbolic curves with Km values of 0.4 and 0.2 mM for fructose 6-phosphate and ATP, respectively. 3-Phosphoglycerate (I0.5 about 0.15 mM) partially inhibited the kinase activity by counteracting the Pi activation. In contrast, the activity of D-fructose-2,6-bisphosphatase (Km 0.38 mM) is strongly inhibited by Pi (I0.5 0.8 mM) lowering its affinity to fructose-2,6-P2 (Km 1.4 mM). 3-Phosphoglycerate activites the enzyme (A0.5 at about 0.3 mM) without causing a significant change in its Km for fructose-2,6-P2. The activities of both of these enzymes in relationship to the metabolic role of D-fructose 2,6-bisphosphate in the germinating seed is discussed.

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Accession: 014830967

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DOI: 10.1016/0304-4165(84)90105-3


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