The affinity of rabbit muscle fructose-bisphosphatase for fructose bisphosphate.
This paper reports that microM concentrations of fructose bisphosphate are titrated by rabbit muscle fructose-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) when the enzyme concentration is varied in the range which secures measurable initial velocities of reaction: a result that can only be explained by supposing that the enzyme has a greater affinity for fructose bisphosphate than suggested by Fernando, J., Enser, M., Pontremoli, S. and Horecker, B.L. (1968) Arch. Biochem. Biophys. 126, 599-606. The results also suggest that the keto form of the substrate may be the preferred configuration and that the enzyme is inhibited by magnesium-bound fructose bisphosphate.
D000818:Animals; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005635:Fructosediphosphates / Q000494:pharmacology*; D006598:Hexosediphosphates / Q000494:pharmacology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011817:Rabbits
D005635:Fructosediphosphates; D006598:Hexosediphosphates; D006597:Fructose-Bisphosphatase; D008274:Magnesium