Fructose-2,6-bisphosphatase is an enzyme that catalyzes the following reaction:
fructose-2,6-bisphosphate + H2O ---> fructose-6-phosphate + phosphate ion
Fructose-2,6-bisphosphatase is important in regulation of gluconeogenesis & glycolysis as it catalyzes the dephosphorylation of fructose-2,6-bisphosphate. Because fructose-2,6-bisphosphate activates phosphofructokinase-1 (a critical enzyme in glycolysis) and inhibits fructose-1,6-bisphosphatase (a critical enzyme in gluconeogenesis), the activity of fructose-2,6-bisphosphatase decreases glycolysis and increases gluconeogenesis.
Fructose-2,6-bisphosphatase is subject to product inhibition by fructose-6-phosphate. Fructose-2,6-bisphosphatase also undergoes addition of a phosphate group to a single serine residue by cAMP-dependent protein kinase (known as covalent modification), which activates (increases catalytic activity) of Fructose-2,6-bisphosphatase.
See also
External links
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Hydrolase: esterases (EC 3.1) |
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| 3.1.1: Carboxylic ester hydrolases |
Cholinesterase ( Acetylcholinesterase, Butyrylcholinesterase) - Pectinesterase - 6-phosphogluconolactonase - PAF acetylhydrolase
Lipase (Gastric/Lingual, Pancreatic, Lysosomal, Hormone-sensitive, Endothelial, Hepatic, Lipoprotein, Monoacylglycerol, Diacylglycerol)
Phospholipase ( A1, A2, B)
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| 3.1.2: Thioesterase |
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| 3.1.3: Phosphatase |
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| 3.1.4: Phosphodiesterase |
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| 3.1.6: Sulfatase |
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| other |
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