PFP (enzyme)

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 $$\rightleftharpoons$$ 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.

Nomenclature
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:D-fructose-6-phosphate 1-phosphotransferase. Other names in common use include:
 * 6-phosphofructokinase (pyrophosphate),
 * inorganic pyrophosphate-dependent phosphofructokinase,
 * inorganic pyrophosphate-phosphofructokinase,
 * pyrophosphate-dependent phosphofructo-1-kinase, and
 * pyrophosphate-fructose 6-phosphate 1-phosphotransferase,
 * pyrophosphate-fructose 6-phosphate phosphotransferase