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A general method has been developed for the synthesis of chiral [16O,17O,18O]phosphate monoesters of known absolute configuration. An analytic method for determining the absolute configuration of chiral phosphate esters has also been developed, which is based on the isotope effects of 17O and 18O at phosphorus in the 31P nuclear magnetic resonance spectrum. These methods have shown that phosphoryl transfer catalysed by hexokinase, phosphofructokinase and pyruvate kinase occurs with inversion of configuration. This is most simply interpreted as an "in-line' transfer of the phosphoryl group between substrates in the enzyme-substrate ternary complex.

More information

DOI

10.1098/rstb.1981.0062

Type

Journal article

Publication Date

26/06/1981

Volume

293

Pages

75 - 92

Total pages

17

Keywords

Animals, Catalysis, Glycolysis, Hexokinase, Magnetic Resonance Spectroscopy, Organophosphates, Organophosphorus Compounds, Oxygen Isotopes, Phosphofructokinase-1, Phosphotransferases, Protein Conformation, Pyruvate Kinase, Stereoisomerism, Substrate Specificity