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Energy transduction at the catalytic site of enzymes: Hydrolysis of phosphoester bonds and synthesis of pyrophosphate by alkaline phosphatase
Author(s) -
Nayudu Ramachandra V.,
de Meis Leopoldo
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81082-8
Subject(s) - pyrophosphate , alkaline phosphatase , phosphodiester bond , chemistry , hydrolysis , catalysis , phosphate , enzyme , phosphoserine , phosphatase , biochemistry , aqueous solution , organic chemistry , serine , rna , gene
Alkaline phosphatase from mouse intestinal epithelial cells catalyzes the synthesis of pyrophosphate from P i during hydrolysis of either glucose 6‐phosphate, ATP, ADP, inorganic pyrophosphate or p ‐nitrophenylphosphate. The rate of pyrophosphate synthesis is increased by MgCl 2 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.