Binding of zinc(II) to beta-D-fructose 2,6-bisphosphate

Biochem Biophys Res Commun. 1987 Feb 27;143(1):206-11. doi: 10.1016/0006-291x(87)90651-6.

Abstract

The formation of a complex between Zn(II) and beta-D-fructose 2,6-bisphosphate was shown because the latter compound: activated bis(5'-guanosyl)tetraphosphatase (EC 3.6.1.17) and dinucleoside triphosphatase (EC 3.6.1.29) only to the extent that they could be inhibited by Zn(II); increased the consumption of Zn(II) necessary to titrate to an end point a solution of the metallochromic indicator eriochrome black T; coeluted with Zn(II) in a gel filtration column capable of resolving them if unbound. Neither of those effects was shown by D-fructose 1,6-bisphosphate under the same conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases*
  • Animals
  • Enzyme Activation
  • Fructosediphosphates* / pharmacology*
  • Hexosediphosphates* / pharmacology*
  • Kinetics
  • Liver / enzymology
  • Organometallic Compounds / pharmacology*
  • Phosphoric Monoester Hydrolases / isolation & purification
  • Phosphoric Monoester Hydrolases / metabolism*
  • Rats
  • Zinc* / pharmacology

Substances

  • Fructosediphosphates
  • Hexosediphosphates
  • Organometallic Compounds
  • fructose 2,6-bisphosphate-zinc(II) complex
  • fructose 2,6-diphosphate
  • Phosphoric Monoester Hydrolases
  • Acid Anhydride Hydrolases
  • bis(5'-nucleosyl)tetraphosphatase (asymmetrical)
  • bis(5'-adenosyl)triphosphatase
  • Zinc