page_title: PFP (enzyme)
hierarchical_section_title: PFP (enzyme)
caption_attribution_description: English: By Richard Wheeler (Zephyris) 2006. For the metabolic pathways wikiproject. en:Category:Protein images
context_page_description: Diphosphate—fructose-6-phosphate 1-phosphotransferase also known as PFP is an enzyme of carbohydrate metabolism in plants and some bacteria. The enzyme catalyses the reversible interconversion of fructose 6-phosphate and fructose 1,6-bisphosphate using inorganic pyrophosphate as the phosphoryl donor:
  diphosphate + D-fructose 6-phosphate phosphate + D-fructose 1,6-bisphosphate
  In plants, the PFP is located in the cytosol of the cell and is strongly activated by the signal molecule fructose 2,6-bisphosphate.
  PFP is an exclusively cytosolic enzyme that catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate in the glycolytic direction, and the de-phosphorylation of fructose-1,6-bisphosphate to fructose-6-phosphate in the gluconeogenic reaction. Reeves first isolated PFP from Entamoeba histolytica, a lower eukaryote. The first plant PFP isolated was from the leaves of pineapples by Carnal and Black and it has since been isolated from a variety of plant species and tissues.
context_section_description: Diphosphate—fructose-6-phosphate 1-phosphotransferase also known as PFP is an enzyme of carbohydrate metabolism in plants and some bacteria. The enzyme (EC 2.7.1.90) catalyses the reversible interconversion of fructose 6-phosphate and fructose 1,6-bisphosphate using inorganic pyrophosphate as the phosphoryl donor:
  diphosphate + D-fructose 6-phosphate  phosphate + D-fructose 1,6-bisphosphate
  In plants, the PFP is located in the cytosol of the cell and is strongly activated by the signal molecule fructose 2,6-bisphosphate.
  PFP is an exclusively cytosolic enzyme that catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate in the glycolytic direction, and the de-phosphorylation of fructose-1,6-bisphosphate to fructose-6-phosphate in the gluconeogenic reaction.  Reeves first isolated PFP from Entamoeba histolytica, a lower eukaryote.  The first plant PFP isolated was from the leaves of pineapples by Carnal and Black and it has since been isolated from a variety of plant species and tissues.
caption: Bacillus stearothermophilus phosphofructokinase.[1]
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