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Pyrophosphate‐dependent phosphofructokinase, an anaerobic glycolytic enzyme?
Author(s) -
Mertens Emmanuel
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80711-b
Subject(s) - phosphofructokinase , pyrophosphate , glycolysis , biochemistry , enzyme , chemistry , phosphofructokinase 1 , phosphofructokinase 2 , anaerobic exercise , biology , physiology
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.