Fructose 2,6-bisphosphate as a contaminant of commercially obtained fructose 6-phosphate: effect on PPi:fructose 6-phosphate phosphotransferase. 1983

N J Kruger, and E Kombrink, and H Beevers

Fructose 6-phosphate from several commercial sources was shown to be contaminated with fructose 2,6-bisphosphate. This contaminant was identified by its activation of PPi:fructose 6-phosphate phosphotransferase, extreme acid lability and behaviour on ion-exchange chromatography. The apparent kinetic properties of PPi:fructose 6-phosphate phosphotransferase from castor bean endosperm were considerably altered when contaminated fructose 6-phosphate was used as a substrate. Varying levels of fructose 2,6-bisphosphate in the substrate may account for differences that have been observed in the properties of the above enzyme from several plant sources.

UI MeSH Term Description Entries
D010744 Phosphoric Monoester Hydrolases A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. Phosphatase,Phosphatases,Phosphohydrolase,Phosphohydrolases,Phosphomonoesterase,Phosphomonoesterases,Phosphoric Monoester Hydrolase,Hydrolase, Phosphoric Monoester,Hydrolases, Phosphoric Monoester,Monoester Hydrolase, Phosphoric
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D002852 Chromatography, Ion Exchange Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins. Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005636 Fructosephosphates
D025481 Phosphofructokinase-2 An allosteric enzyme that regulates glycolysis and gluconeogenesis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-2,6-bisphosphate, an allosteric effector for the other 6-phosphofructokinase, PHOSPHOFRUCTOKINASE-1. Phosphofructokinase-2 is bifunctional: the dephosphorylated form is a kinase and the phosphorylated form is a phosphatase that breaks down fructose-2,6-bisphosphate to yield fructose-6-phosphate. 6-Phosphofructo-2-kinase,6-Phosphofructo-2-kinase-fructose-2,6-bisphosphatase,Fructose-2,6-bisphosphatase,6-PF-2-K-Fru-2,6-P(2)ase,6-Phosphofructo 2-kinase-fructose 2,6-bisphosphatase,6PF2K,ATP-D-Fructose-6-phosphate 2-phosphotransferase,F Kinase-F-bisphosphatase,Fru-6-P,2-kinase,Fru-kinase-Fru-bisphosphatase,Fructose 2,6-bisphosphatase,Fructose-2,6-bisphosphate 2-phosphatase,Fructose-6-P,2-kinase,Fructose-6-phosphate,2-kinase,Fructose-6-phosphate,2-kinase-fructose-2,6-bisphosphatase,fructose-2,6-diphosphatase,Phosphofructokinase 2

Related Publications

N J Kruger, and E Kombrink, and H Beevers
February 1993, Archives of biochemistry and biophysics,
N J Kruger, and E Kombrink, and H Beevers
December 1981, Biochemical and biophysical research communications,
N J Kruger, and E Kombrink, and H Beevers
March 1982, Molecular and cellular endocrinology,
N J Kruger, and E Kombrink, and H Beevers
January 1988, Biomedica biochimica acta,
Copied contents to your clipboard!