Fructose 1,6-bisphosphatase (FBPase; EC 126.96.36.199) is an enzyme in the liver that converts fructose-1,6-bisphosphate to fructose 6-phosphate in gluconeogenesis. Fructose bisphosphatase catalyses the reverse of the reaction which is catalysed by phosphofructokinase, which is involved in the process of glycolysis. These enzymes only catalyse the reaction in one direction each, and are regulated by metabolites such as fructose 2,6-bisphosphate so that high activity of one of the two enzymes is accompanied by low activity of the other. It is involved in many different metabolic pathways and found in most organisms. FBPase requires metal ions for catalysis (Mg2+ and Mn2+ being preferred) and the enzyme is potently inhibited by Li+.
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|Molecular Weight:||36.8 kDa|
|Buffer:||50 mM potassium phosphate pH-7.4, 50 mM sodium chloride, 0.5 mM ethylenediaminetetraaceticacid, and 2.5% glycerol.|
|Comments:||Fructose 1,6 biphosphatase, (Eur. J. Med Chem. 45:1478, 2009), aa 338 (full length), MW= 36.8 kDa, expressed in E.coli.|
|Storage:||Stable for > 6 months at -80C|
Specific Activity: 1525 pmol/min/ug. One unit is defined as the amount of enzyme that will convert 1 nmol of NADP to NADPH at 30 oC. Assay conditions: 25 mM HEPES, pH7.5, 2mM MgCl2, 2 mM ammonium sulfate, 0.2 mM NADP, 0.05 mM EDTA, 1 mM dithiothreitol, 100 µM fructose-6-biphosphate, 20 units/ml glucose 6-phosphate dehydrogenase, 20 units/ml phosphoglucose isomerase, 100 µg/ml bovine serum albumin, and 10 nM fructose 1,6 biphosphatase at 30 oC for 30 min.
Mass Spectroscopy: MALDI-TOF MW 36.7 kDa
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