PFP (enzyme)
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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
Diphosphate—fructose-6-phosphate 1-phosphotransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.1.90 | ||||||||
CAS no. | 55326-40-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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[2] first isolated PFP from Entamoeba histolytica, a lower eukaryote. The first plant PFP isolated was from the leaves of pineapples by Carnal and Black[3] and it has since been isolated from a variety of plant species and tissues.[4]