Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1098/rstb.1981.0062

Type

Journal article

Journal

Philosophical transactions of the Royal Society of London. Series B, Biological sciences

Publication Date

06/1981

Volume

293

Pages

75 - 92

Keywords

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