Allosteric regulatory properties of muscle phosphofructokinase.
We have reviewed the allosteric regulatory properties of skeletal muscle phosphofructokinase and recent results on the phosphorylation of this enzyme. The number and affinities of various ligand binding sites are described, and a simple three state model is presented to explain the kinetic and ligand-binding properties of the enzyme. Data describing a lack of fit to a concerted transition model are presented. The widespread occurrence of partial phosphorylation of phosphofructokinase at a specific site near the carboxyl terminus is documented, as well as the lack of significant kinetic consequences of such phosphorylation.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D009132:Muscles / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010748:Phosphopeptides / Q000032:analysis; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
D000596:Amino Acids; D008024:Ligands; D010748:Phosphopeptides; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D010732:Phosphofructokinase-1