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Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase

An Erratum to this article was published on 26 October 1978


THE recent synthesis and stereochemical analysis of a phosphate monoester chiral at phosphorus by virtue only of the three stable isotopes of oxygen1,2 opens the way to the determination of the stereochemical course of both chemical and enzymatic reactions that involve the transfer of a phosphoryl group. We report here the first determination of the stereochemical consequence at phosphorus of an intermolecular phosphoryl transfer reaction. In studying the reaction catalysed by alkaline phosphatase we had two aims: first, to discover the stereochemical course of this well-studied transfer, and second to devise a general method by which the configuration of any chiral phosphate monoester can be determined.

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JONES, S., KINDMAN, L. & KNOWLES, J. Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase. Nature 275, 564–565 (1978).

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