Energy transduction at the catalytic site of enzymes: hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase

FEBS Lett. 1989 Sep 11;255(1):163-6. doi: 10.1016/0014-5793(89)81082-8.


Alkaline phosphatase from mouse intestinal epithelial cells catalyzes the synthesis of pyrophosphate from Pi during hydrolysis of either glucose 6-phosphate, ATP, ADP, inorganic pyrophosphate or p-nitrophenylphosphate. The rate of pyrophosphate synthesis is increased by MgCl2 and by decreasing the pH of the medium from 8.5 to 6.0. The data presented indicate that at the catalytic site of alkaline phosphatase the energies of hydrolysis of the phosphoserine residue and of pyrophosphate are different from those measured in aqueous solutions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Alkaline Phosphatase / metabolism*
  • Animals
  • Binding Sites
  • Catalysis
  • Diphosphates / metabolism*
  • Energy Transfer
  • Hydrolysis
  • Intestinal Mucosa / enzymology
  • Mice
  • Phosphoserine / metabolism*
  • Serine
  • Water


  • Diphosphates
  • Water
  • Phosphoserine
  • Serine
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Alkaline Phosphatase