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Moss phosphofructokinase is less sensitive than other plant phosphofructokinases to inhibition by phosphoenolpyruvate
Author(s) -
Kelly Grahame J.,
Latzko Erwin
Publication year - 1981
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1981.tb06051.x
Subject(s) - phosphofructokinase , phosphoenolpyruvate carboxykinase , moss , chlorella , enzyme , chemistry , botany , biochemistry , biology , algae , glycolysis
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.