Abstract
Inorganic pyrophosphate:D-fructose-6-phosphate 1-phosphotransferase from mung beans ( Phaseolus aureus Roxb. ) was activated markedly by D-fructose 2,6-bisphosphate, with a K A of about 50 nM. The enzyme exhibited hyperbolic kinetics both in the absence and presence of the activator. D-Fructose 2,6-bisphosphate (1 μM) decreased the K m for D-fructose 6-phosphate 67-fold (from 20 mM to 0.3 mM) and increased the V max 15-fold; these two effects combined to give a 500-fold activation at 0.3 mM D-fructose 6-phosphate. In contrast, ATP:D-fructose 6-phosphate 1-phosphotransferase from the same source was found not to be affected by D-fructose 2,6-bisphosphate. A natural activator for inorganic pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase was isolated from mung-bean extracts and identified as D-fructose 2,6-bisphosphate.
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More From: Biochemical and Biophysical Research Communications
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