Influence of ATP and magnesium on phosphofructokinase from sea bass (Dicentrarchus labrax L.) liver.
Glycolytic enzyme phosphofructokinase (PFK) from sea-bass liver shows inhibition for ATP4- and MG-ATP2-, and ATP4- is a competitive inhibitor with respect to MG-ATP2-. Free Mg2+ behaves as a mixed inhibitor on the kinetic with respect to the true enzyme substrate Mg-ATP2-, and eliminates the inhibition effect of this substrate. The kinetics with respect to Mg-ATP2- at non-inhibiting concentrations is not visibly affected by temperature of pH variation. The inhibiting effect of Mg-ATP2- is more marked at 22 and 10 degrees C (of three assayed temperatures 22, 15 and 10 degrees C and at physiological pH 6.8) as opposed to the maximum activity pH (8.0).
Fideu
M D
MD
Herranz
M J
MJ
Ruíz-Amil
M
M
Pérez
M L
ML
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013696:Temperature
D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; D008274:Magnesium