title: Stereochemical course of phospho group transfer by human prostatic acid phosphatase.
abstract: The stereochemical course of the phospho transfer catalyzed by homogeneous human prostatic acid phosphatase was investigated using 31P nuclear magnetic resonance spectroscopy. Transphosphorylation from phenyl-(R)-[15O, 17O, 18O]phosphate to (S)-propane-1,2-diol occurs with overall retention of configuration at phosphorus. This stereochemical result is consistent with the interpretation that the hydrolysis of substrates by this enzyme proceeds by way of a covalent phosphoenzyme intermediate. Conditions for optimizing phospho transfer by this and related acid phosphatases have also been explored.
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D010103:Oxygen Isotopes; D010766:Phosphorylation; D011467:Prostate / Q000201:enzymology*; D011485:Protein Binding; D013237:Stereoisomerism
chemical_list: D010103:Oxygen Isotopes; D000135:Acid Phosphatase