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Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinases catalyse the transfer of the chiral [16O,17O,18O]phosphoryl group from D-fructose 1[(S)-16O,17O,18O],6-bisphosphate to ADP with inversion of configuration at the phosphorus atom. D-Fructose 1[(S)-16O,17O,18O],-bisphosphate was synthesized in situ from sn-glycerol 3[(S)-16O,17O,18O]phosphate. The simplest interpretation of these results is that the phosphoryl group is transferred between substrates in the enzyme substrate ternary complexes by an 'in-line' mechanism.

Original publication

DOI

10.1042/bj1990427

Type

Journal article

Journal

The Biochemical journal

Publication Date

11/1981

Volume

199

Pages

427 - 432

Keywords

Muscles, Animals, Rabbits, Oxygen Isotopes, Phosphofructokinase-1, Glycerophosphates, Fructosediphosphates, Adenosine Triphosphate, Magnetic Resonance Spectroscopy, Phosphorylation, Stereoisomerism, Geobacillus stearothermophilus