Crystal structure of a trapped phosphoenzyme during a catalytic reaction

Nat Struct Biol. 1997 Aug;4(8):615-8. doi: 10.1038/nsb0897-615.

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

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalysis
  • Crystallography, X-Ray
  • Enzyme Inhibitors / pharmacology
  • Fructosediphosphates / chemistry*
  • Fructosediphosphates / metabolism
  • Fructosephosphates / pharmacology
  • Liver / enzymology
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Phosphofructokinase-2
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Phosphoric Monoester Hydrolases / antagonists & inhibitors
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / metabolism
  • Rats

Substances

  • Enzyme Inhibitors
  • Fructosediphosphates
  • Fructosephosphates
  • Phosphoproteins
  • fructose-6-phosphate
  • fructose 2,6-diphosphate
  • Phosphofructokinase-2
  • Phosphoric Monoester Hydrolases