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词条 PFP (enzyme)
释义

  1. Nomenclature

  2. See also

  3. References

  4. Further reading

{{Distinguish|Perforin}}{{enzyme
| Name = Diphosphate—fructose-6-phosphate 1-phosphotransferase
| EC_number = 2.7.1.90
| CAS_number = 55326-40-4
| IUBMB_EC_number = 2/7/1/90
| GO_code = 0047334
| image = Phosphofructokinase 6PFK wpmp.png
| width =
| caption = Bacillus stearothermophilus phosphofructokinase.[1]
}}

Diphosphate—fructose-6-phosphate 1-phosphotransferase also known as PFP is an enzyme of carbohydrate metabolism in plants and some bacteria. The enzyme ({{EC_number|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[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

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

  • PFK

References

1. ^{{PDB|6PFK}}; {{cite journal |vauthors=Schirmer T, Evans PR | title = Structural basis of the allosteric behaviour of phosphofructokinase | journal = Nature | volume = 343 | issue = 6254 | pages = 140–5 |date=January 1990 | pmid = 2136935 | doi = 10.1038/343140a0 | url = }}
2. ^{{cite journal |vauthors=Reeves RE, South DJ, Blytt HJ, Warren LG | title = Pyrophosphate:D-fructose 6-phosphate 1-phosphotransferase. A new enzyme with the glycolytic function of 6-phosphofructokinase | journal = J. Biol. Chem. | volume = 249 | issue = 24 | pages = 7737–41 |date=December 1974 | pmid = 4372217 | doi = | url = }}
3. ^{{cite journal |vauthors=Carnal NW, Black CC | title = Pyrophosphate-dependent 6-phosphofructokinase, a new glycolytic enzyme in pineapple leaves | journal = Biochem. Biophys. Res. Commun. | volume = 86 | issue = 1 | pages = 20–6 |date=January 1979 | pmid = 219853 | doi = 10.1016/0006-291X(79)90376-0| url = }}
4. ^{{cite journal | author = Stitt M|date=June 1990 | title = Fructose-2,6-Bisphosphate as a Regulatory Molecule in Plants | journal = Annual Review of Plant Physiology and Plant Molecular Biology | volume = 41 | pages = 153–185 | doi = 10.1146/annurev.pp.41.060190.001101 }}

Further reading

{{refbegin}}
  • {{cite journal |vauthors=Reeves RE, Serrano R, South DJ | date = 1976 | title = 6-phosphofructokinase (pyrophosphate). Properties of the enzyme from Entamoeba histolytica and its reaction mechanism | journal = J. Biol. Chem. | volume = 251 | pages = 2958–62 | pmid = 178659 | issue = 10 }}
{{refend}}{{Kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{DEFAULTSORT:Pfp (Enzyme)}}{{2.7-enzyme-stub}}

1 : EC 2.7.1

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