title: Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast.
abstract: Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.
authors.affiliation: Institute of Biochemistry, Karl-Marx-University Leipzig, German Democratic Republic.
authors.forename: M
authors.initials: M
authors.lastname: Kretschmer
authors.forename: W
authors.initials: W
authors.lastname: Schellenberger
authors.forename: A
authors.initials: A
authors.lastname: Otto
authors.forename: R
authors.initials: R
authors.lastname: Kessler
authors.forename: E
authors.initials: E
authors.lastname: Hofmann
mesh_terms: D002846:Chromatography, Affinity; D005635:Fructosediphosphates / Q000378:metabolism; D005636:Fructosephosphates / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D005635:Fructosediphosphates; D005636:Fructosephosphates; D010710:Phosphates; C027618:fructose-6-phosphate; C027652:fructose 2,6-diphosphate; D017853:Phosphotransferases (Alcohol Group Acceptor); D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases