Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphatase.
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.
D000469:Alkaline Phosphatase / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D009154:Mutation; D010766:Phosphorylation; D013237:Stereoisomerism
D000469:Alkaline Phosphatase