The inhibition of fructose 1,6-bisphosphatase by fructose 2,6-bisphosphate is enhanced by EDTA and diminished by zinc(II)

Biochem Int. 1988 Apr;16(4):747-53.

Abstract

The sensitivity of the Mg(II)-dependent activity of rabbit liver fructose 1,6-bisphosphatase (FBPase, EC 3.1.3.11) to inhibition by fructose 2,6-bisphosphate (Fru-2,6-P2) was enhanced by EDTA and diminished to negligible levels by 0.5-2 microM Zn(II) added as another FBPase inhibitor. Fru-2,6-P2 was more efficient in the presence of the synergistic effector AMP: still, the Fru-2,6-P2 concentration inhibiting 50% changed from 3 microM (with EDTA) to higher than 50 microM (with Zn(II]. On the other hand, the Zn(II)-dependent FBPase activity was inhibited by Fru-2,6-P2 to a much lesser extent than the Mg(II)-dependent activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Monophosphate / pharmacology
  • Animals
  • Edetic Acid / pharmacology
  • Fructose-Bisphosphatase / antagonists & inhibitors*
  • Fructosediphosphates / pharmacology*
  • Hexosediphosphates / pharmacology*
  • In Vitro Techniques
  • Kinetics
  • Liver / enzymology
  • Magnesium / pharmacology
  • Rabbits
  • Zinc / pharmacology

Substances

  • Fructosediphosphates
  • Hexosediphosphates
  • Adenosine Monophosphate
  • fructose 2,6-diphosphate
  • Edetic Acid
  • Fructose-Bisphosphatase
  • Magnesium
  • Zinc