Abstract
The crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water.
Publication types
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Letter
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Catalysis
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Crystallography, X-Ray
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Enzyme Inhibitors / pharmacology
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Fructosediphosphates / chemistry*
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Fructosediphosphates / metabolism
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Fructosephosphates / pharmacology
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Liver / enzymology
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Models, Molecular
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Molecular Conformation
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Molecular Sequence Data
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Phosphofructokinase-2
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Phosphoproteins / chemistry*
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Phosphoproteins / metabolism
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Phosphoric Monoester Hydrolases / antagonists & inhibitors
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Phosphoric Monoester Hydrolases / chemistry*
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Phosphoric Monoester Hydrolases / metabolism
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Rats
Substances
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Enzyme Inhibitors
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Fructosediphosphates
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Fructosephosphates
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Phosphoproteins
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fructose-6-phosphate
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fructose 2,6-diphosphate
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Phosphofructokinase-2
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Phosphoric Monoester Hydrolases