Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase |
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| Authors: | J E Butler-Ransohoff D A Kendall S Freeman J R Knowles E T Kaiser |
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| Institution: | Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, New York 10021. |
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| 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. |
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