Stereochemistry of phospho transfer catalyzed by bovine liver acid phosphatase.
The hydrolysis of phosphoric monoesters by acid phosphatases is thought to proceed via the formation of a phosphoenzyme intermediate, but no stereochemical evidence exists on this point. We have carried out the transphosphorylation from phenyl (R)-[16O, 17O, 18O] phosphate to (S)-propane-1,2-diol in the presence of homogeneous bovine liver acid phosphatase, and have found that the reaction proceeds with greater 90% overall retention of configuration at phosphorus. This stereochemical course of phospho transfer during the enzyme-catalyzed reaction of the phosphoric monoester is consistent with a double displacement mechanism in which each step proceeds with inversion of the stereochemistry at phosphorus, and is similar to the behavior of the bacterial alkaline phosphatase.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D007536:Isomerism; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D010755:Organophosphates; D009943:Organophosphorus Compounds; D010103:Oxygen Isotopes
D010755:Organophosphates; D009943:Organophosphorus Compounds; D010103:Oxygen Isotopes; D000135:Acid Phosphatase; C005445:triphenyl phosphate