Moss phosphofructokinase is less sensitive than other plant phosphofructokinases to inhibition by phosphoenolpyruvate [Brachytecium rutabulum, spinach, Chlorella, Mnium hornum, glycolysis]
1981
Kelly, G.J. (New England Univ., Armidale (Australia). Dept. of Biochemistry and Nutrition) | Latzko, E.
Phosphofructokinase was partially purified from the moss Brachythecium rutabulum (Hedw). Br. Eur. and found not to be inhibited by 400 mu-M phospgoenolpyruvate, whereas spinach and Chlorella phosphofructokinases were inhibited over 80 per cent by phosphoenolpyruvate at one-fifth of this concentration. Mixing experiments indicated that the insensitivity of the moss phosphofructokinase was not an artifact of the extraction procedure. Other kinetic and regulatory properties of moss phosphofructokinase were similar to those reported for the enzyme from other plants.
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