Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?
Recent evidence indicates that in as diverse organisms as unicellular eukaryotes, higher plants and prokaryotes, anaerobic glycolysis relies on a pyrophosphate-dependent phosphofructokinase instead of the classical ATP-dependent enzyme. This difference in phosphoryl donor specificity does not necessarily reflect a primitive metabolism, as thought earlier, but could rather be the result of convergent evolution, fostered by the energetic advantage conferred to the cell when glycolysis is the sole source of ATP.
Mertens
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Rockefeller University, New York, NY 10021.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000693:Anaerobiosis; D005075:Biological Evolution; D011756:Diphosphates / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism; D005636:Fructosephosphates / Q000378:metabolism*; D006019:Glycolysis; D010770:Phosphotransferases / Q000378:metabolism*; D010802:Phylogeny; D010944:Plants / Q000378:metabolism; D011387:Prokaryotic Cells / Q000378:metabolism
D011756:Diphosphates; D005636:Fructosephosphates; C027618:fructose-6-phosphate; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; C022502:pyrophosphate-fructose 6-phosphate 1-phosphotransferase