| Title | Stereochemical course of phospho group transfer by human prostatic acid phosphatase. |
| Publication Type | Journal Article |
| Year of Publication | 1984 |
| Authors | Buchwald SL, Saini MS, Knowles JR, Van Etten RL |
| Journal | J Biol Chem |
| Volume | 259 |
| Issue | 4 |
| Pagination | 2208-13 |
| Date Published | 1984 Feb 25 |
| ISSN | 0021-9258 |
| Keywords | Acid Phosphatase, Humans, Kinetics, Magnetic Resonance Spectroscopy, Male, Oxygen Isotopes, Phosphorylation, Prostate, Protein Binding, Stereoisomerism |
| 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. |
| Alternate Journal | J Biol Chem |
| PubMed ID | 6698963 |
| Grant List | GM 21659 / GM / NIGMS NIH HHS / United States GM 27003 / GM / NIGMS NIH HHS / United States RR 01077 / RR / NCRR NIH HHS / United States |