Pyrophosphate dependent phosphofructokinase

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Pyrophosphate dependent phosphofructokinase (also known as pyrophosphate: fructose-6-phosphate 1-phosphotransferase, PFP or PPi-PFK, EC 2.7.1.90) is an enzyme that catalyses the interconversion of fructose-6-phosphate (F6P) and fructose-1,6-bisphosphate (F16bP) using pyrophosphate (PPi) in the forward (phosphorylating) reaction.

[edit] Characteristics

Most plant-derived PFPs are strongly activated and tightly regulated by fructose-2,6-bisphosphate (F26bP). Active plant PFP is tetrameric, with few exceptions, and consists of two alpha- and two beta subunits. Non-plant PFPs are often dimeric with two identical subunits.

Giardia lamblia, a flagellated, unicellular organism, possesses a PFP that is not affected by F26bP. DNA sequencing has shown that the subunit of Giardia lamblia PFP corresponds to the alpha subunit of tetrameric plant PFPs, while the beta subunit contains the F26bP binding site. Ongoing research on the mechanism of action in plants show that F26bP may induce two Alpha-Beta dimers to form a 2Alpha-2Beta tetramer that is catalytically active.

[edit] History

PFP was discovered in pineapple leaves by Carnal and Black (1979) and has since been discovered in many plants and microorganisms.

[edit] References

Carnal NW, Black CC. (1979) Pyrophosphate-dependent 6-phosphofructokinase, a new glycolytic enzyme in pineapple leaves. Biochemical and biophysical research communications. 86: 20 26.