Moss phosphofructokinase is less sensitive than other plant phosphofructokinases to inhibition by phosphoenolpyruvate |
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| Authors: | Grahame J Kelly Erwin Latzko |
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| Institution: | Department of Biochemistry and Nutrition, University of New England, Armidale, N.S.W. 2351, Australia;Botanisches Institut der Universität, Schlossgarten 3f D-4400 Münster, Federal Republic of Germany. |
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| Abstract: | Phosphofructokinase was partially purified from the moss Brachythecium rutabulum (Hedw.) Bt. Eur. and found not to be inhibited by 400 μ M phosphoenolpyruvate, whereas spinach and Chlorella phosphofructokinases were inhibited over 80% 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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| Keywords: | Glycolysis moss phosphoenolpyruvate phosphofructokinase |
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