PFP (enzyme)

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Diphosphate—fructose-6-phosphate 1-phosphotransferase
Phosphofructokinase 6PFK wpmp.png
Bacillus stearothermophilus phosphofructokinase.[1]
Identifiers
EC number 2.7.1.90
CAS number 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 / EGO

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 \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-bisphoshate 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]

Nomenclature[edit]

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

See also[edit]

References[edit]

  1. ^ PDB 6PFK; Schirmer T, Evans PR (January 1990). "Structural basis of the allosteric behaviour of phosphofructokinase". Nature 343 (6254): 140–5. doi:10.1038/343140a0. PMID 2136935. 
  2. ^ 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. PMID 4372217. 
  3. ^ 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. PMID 219853. 
  4. ^ Stitt M (June 1990). "Fructose-2,6-Bisphosphate as a Regulatory Molecule in Plants". Annual Review of Plant Physiology and Plant Molecular Biology 41: 153–185. doi:10.1146/annurev.pp.41.060190.001101. 

Further reading[edit]

  • 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. PMID 178659.