Abstract
Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
MeSH terms
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Chromatography, Affinity
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Fructosediphosphates / metabolism
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Fructosephosphates / metabolism
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Phosphates / metabolism
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Phosphofructokinase-2
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Phosphoric Monoester Hydrolases / antagonists & inhibitors
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Phosphoric Monoester Hydrolases / isolation & purification*
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Phosphoric Monoester Hydrolases / metabolism
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Phosphotransferases (Alcohol Group Acceptor) / antagonists & inhibitors
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Phosphotransferases (Alcohol Group Acceptor) / isolation & purification*
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Saccharomyces cerevisiae / enzymology*
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Substrate Specificity
Substances
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Fructosediphosphates
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Fructosephosphates
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Phosphates
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fructose-6-phosphate
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fructose 2,6-diphosphate
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Phosphotransferases (Alcohol Group Acceptor)
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Phosphofructokinase-2
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Phosphoric Monoester Hydrolases