Binding of zinc(II) to beta-D-fructose 2,6-bisphosphate.
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.
D017766:Acid Anhydride Hydrolases; D000818:Animals; D004789:Enzyme Activation; D005635:Fructosediphosphates / Q000494:pharmacology*; D006598:Hexosediphosphates / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009942:Organometallic Compounds / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D015032:Zinc / Q000494:pharmacology; D000099170:Bis(5'-adenosyl)triphosphatase
D017766:Acid Anhydride Hydrolases; D005635:Fructosediphosphates; D006598:Hexosediphosphates; D009942:Organometallic Compounds; D010744:Phosphoric Monoester Hydrolases; D015032:Zinc; D000099170:Bis(5'-adenosyl)triphosphatase; C051849:fructose 2,6-bisphosphate-zinc(II) complex; C027652:fructose 2,6-diphosphate; C020023:bis(5'-nucleosyl)tetraphosphatase (asymmetrical)