Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?

FEBS Lett. 1991 Jul 8;285(1):1-5. doi: 10.1016/0014-5793(91)80711-b.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Anaerobiosis
  • Biological Evolution
  • Diphosphates / metabolism
  • Eukaryotic Cells / metabolism
  • Fructosephosphates / metabolism*
  • Glycolysis*
  • Phosphotransferases / metabolism*
  • Phylogeny
  • Plants / metabolism
  • Prokaryotic Cells / metabolism

Substances

  • Diphosphates
  • Fructosephosphates
  • fructose-6-phosphate
  • Adenosine Triphosphate
  • Phosphotransferases
  • pyrophosphate-fructose 6-phosphate 1-phosphotransferase