The stereochemical course of phosphoryl transfer catalysed by Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinase with a chiral [16O,17O,18O]phosphate ester.
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.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005635:Fructosediphosphates / Q000378:metabolism; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D005994:Glycerophosphates / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D009132:Muscles / Q000201:enzymology*; D010103:Oxygen Isotopes; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits; D013237:Stereoisomerism
D005635:Fructosediphosphates; D005994:Glycerophosphates; D010103:Oxygen Isotopes; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; C029063:fructose-1,6-diphosphate