Phosphofructokinase from mantle tissue of Mytilus galloprovincialis. Purification and effects of phosphorylation on the enzymatic activity.
Phosphofructokinase purified from mantle tissue of the sea mussel Mytilus galloprovincialis, was phosphorylated "in vitro" by the catalytic subunit of cyclic AMP-dependent protein kinase. The incorporation of phosphate gave rise to an activation of the enzyme by increasing its affinity for fructose-6-phosphate, by decreasing its sensitivity to the inhibition by ATP and by enhancing the effect of allosteric activators (5'-AMP and fructose-2,6-bisphosphate). In addition, the effects of phosphorylation on the catalytic activity are pH-dependent.
Departamento de Bioquímica e Bioloxía Molecular, Facultade de Veterinaria, Universidade de Santiago de Compostela, Lugo, Spain.
M
M
Fernández
J
J
Cao
M D
MD
Vázquez-Illanes
J I
JI
Ramos-Martínez
J A
JA
Villamarín
D000818:Animals; D049872:Bivalvia; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005629:Frozen Sections; D005636:Fructosephosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000302:isolation & purification* / Q000378:metabolism; D010766:Phosphorylation; D014021:Tissue Preservation
D005636:Fructosephosphates; C027618:fructose-6-phosphate; D010732:Phosphofructokinase-1; D017868:Cyclic AMP-Dependent Protein Kinases