Citrate inhibition of rat-kidney cortex phosphofructokinase

Mol Cell Biochem. 1994 Jun 29;135(2):123-8. doi: 10.1007/BF00926514.


The regulatory properties of citrate on the activity of phosphofructokinase (PFK) purified from rat-kidney cortex has been studied. Citrate produces increases in the K0.5 for Fru-6-P and in the Hill coefficient as well as a decrease in the Vmax of the reaction without affecting the kinetic parameters for ATP as substrate. ATP potentiates synergistically the effects of citrate as an inhibitor of the enzyme. Fru-2,6-P2 and AMP at concentrations equal to Ka were not able to completely prevent citrate inhibition of the enzyme. Physiological concentrations of ATP and citrate produce a strong inhibition of renal PFK suggesting that may participate in the control of glycolysis in vivo.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Adenosine Triphosphate / pharmacology
  • Animals
  • Citrates / pharmacology*
  • Citric Acid
  • Fructosephosphates / analysis
  • Kidney Cortex / drug effects*
  • Kidney Cortex / enzymology
  • Kinetics
  • Male
  • Phosphofructokinase-1 / antagonists & inhibitors*
  • Rats
  • Rats, Wistar


  • Citrates
  • Fructosephosphates
  • Citric Acid
  • fructose-6-phosphate
  • Adenosine Triphosphate
  • Phosphofructokinase-1