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 (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

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

References

↑ 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.
↑ 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.
↑ 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.
↑ 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.

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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PFP (enzyme)

Nomenclature

See also

References

Further reading