Binding of fructose 2,6-bisphosphate to yeast phosphofructokinase.
Binding of Fru-2,6-P2 to yeast phosphofructokinase was investigated by ultrafiltration technique. Per mol of subunit of phosphofructokinase (M = 100,000) 0.5 moles of Fru-2,6-P2 are bound. The binding curve proceeds cooperatively (nH = 1.8 +/- 0.2). The apparent affinity constant of Fru-2,6-P2 amounts to about 2.25 +/- 0.12 microM. Fru-1,6-P2 decreases the affinity of yeast phosphofructokinase to Fru-2,6-P2. The data can be described by assuming either competition of Fru-2,6-P2 and Fru-1,6-P2 for the same binding site or conformationally mediated interactions.
Kessler
R
R
Institut für Biochemie, Karl-Marx Universität Leipzig, DDR.
Schellenberger
W
W
Nissler
K
K
Hofmann
E
E
D005635:Fructosediphosphates / Q000378:metabolism* / Q000494:pharmacology; D006598:Hexosediphosphates / Q000378:metabolism*; D008433:Mathematics; D008954:Models, Biological; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005635:Fructosediphosphates; D006598:Hexosediphosphates; C027652:fructose 2,6-diphosphate; D010732:Phosphofructokinase-1; C029063:fructose-1,6-diphosphate