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Rabbit muscle phosphoglucomutase converts alpha-D-glucose 1-[(S)-16O,17O,18O]phosphate into D-glucose 6-[16O,17O,18O]phosphate, which is shown by 31P n.m.r. spectroscopy, after cyclization and methylation, to have the (S)-configuration at the phosphorus atom. Since phosphoglucomutase is known to catalyse phosphoryl transfer by way of a phospho-enzyme intermediate, and since individual phosphoryl-transfer steps appear in general to occur with inversion of configuration, this observation is most simply interpreted in terms of a double-displacement mechanism with two phosphoryl-transfer steps.

Original publication




Journal article


The Biochemical journal

Publication Date





693 - 698


Muscles, Animals, Rabbits, Oxygen Isotopes, Phosphoglucomutase, Glucosephosphates, Glucose-6-Phosphate, Magnetic Resonance Spectroscopy, Molecular Conformation, Phosphorylation, Models, Biological