Structural highlights
Function
PFP1_TRIV3 Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01979][1]
References
- ↑ Mertens E, Van Schaftingen E, Müller M. Presence of a fructose-2,6-bisphosphate-insensitive pyrophosphate: fructose-6-phosphate phosphotransferase in the anaerobic protozoa Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma. Mol Biochem Parasitol. 1989 Dec;37(2):183-90. PMID:2558319 doi:10.1016/0166-6851(89)90150-3
