Effects of phosphorylation on the kinetic properties of rat liver fructose-1,6-bisphosphatase.
A new purification procedure for rat liver fructose-1,6-bisphosphatase that involves use of Procion Red-Sepharose is described. The purified enzyme was homogeneous, had a subunit Mr of 40 000-41 000 and seemed to be undegraded. The enzyme could be phosphorylated by cyclic AMP-dependent protein kinase with a stoicheiometry of one per subunit. Phosphorylation caused a 2-fold decrease in the Km of the enzyme for fructose 1,6-bisphosphate, but did not affect its allosteric responses to AMP, Mg2+ and fructose 2,6-bisphosphate.
D000818:Animals; D002846:Chromatography, Affinity; D006597:Fructose-Bisphosphatase / Q000302:isolation & purification / Q000378:metabolism*; D005635:Fructosediphosphates / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains; D014227:Triazines
D005635:Fructosediphosphates; D014227:Triazines; C020795:procion red HE-3B; D006597:Fructose-Bisphosphatase; C029063:fructose-1,6-diphosphate