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Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase
J E Butler-Ransohoff1, D A Kendall, S Freeman
1Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, New York 10021.
Biochemistry
|June 28, 1988
Abstract:
The stereochemical course of the phospho group transfer catalyzed by mutant (S102C) alkaline phosphatase from Escherichia coli was investigated by using 31P nuclear magnetic resonance spectroscopy. Transphosphorylation from 4-nitrophenyl (Rp)-[16O, 17O, 18O]phosphate to (S)-propane-1,2-diol occurs with overall retention of configuration at phosphorus. This result is consistent with the view that the hydrolysis of substrates by this mutant enzyme proceeds by way of a covalent phosphoenzyme intermediate in the same manner as the wild-type alkaline phosphatase.