PFP is an exclusively cytosolicenzyme 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-bisphoshate 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.
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:
^Reeves RE, South DJ, Blytt HJ, Warren LG (December 1974). "Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase". J. Biol. Chem.249 (24): 7737–41. PMID4372217.
^Carnal NW, Black CC (January 1979). "Pyrophosphate-dependent 6-phosphofructokinase, a new glycolytic enzyme in pineapple leaves". Biochem. Biophys. Res. Commun.86 (1): 20–6. doi:10.1016/0006-291X(79)90376-0. PMID219853.
^Stitt M (June 1990). "Fructose-2,6-Bisphosphate as a Regulatory Molecule in Plants". Annual Review of Plant Physiology and Plant Molecular Biology41: 153–185. doi:10.1146/annurev.pp.41.060190.001101.
Reeves RE, Serrano R, South DJ (1976). "6-phosphofructokinase (pyrophosphate). Properties of the enzyme from Entamoeba histolytica and its reaction mechanism". J. Biol. Chem.251 (10): 2958–62. PMID178659.