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The regulation of the Fru-6-P/Fru-2,6-P2 cycle by the cooperation of allosteric and covalent mechanisms was investigated in a reconstituted enzyme system under in vitro conditions. Phosphorylation of the bifunctional enzyme exerts a much stronger effect than sn-glycerol 3-phosphate in lowering the quasi-stationary concentration of fructose 2,6-bisphosphate and in increasing the critical concentration of the fructose phosphates, respectively. However, sn-glycerol 3-phosphate is able to strongly amplify the decrease of the quasi-stationary concentration of fructose 2,6-bisphosphate due to phosphorylation. The experiments can be described by a mathematical model involving rate equations for the dephosphorylated and the phosphorylated PFD-2 and FBPase-2. The results are compared with data from the literature obtained under in vivo conditions.
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
March 1982,
Molecular and cellular endocrinology,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
January 1981,
Current topics in cellular regulation,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
August 1981,
Biochemical and biophysical research communications,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
April 1984,
The Journal of biological chemistry,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
January 1984,
Biomedica biochimica acta,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
January 1985,
Biomedica biochimica acta,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
November 1995,
Plant physiology,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
October 1992,
The Journal of biological chemistry,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
June 1983,
Biochemical Society transactions,
J Frenzel, and
W Schellenberger, and
K Eschrich, and
E Hofmann
November 1983,
Biochemical and biophysical research communications,
