-transparent.png){kind=logo}
ADP was found to activate or, depending on the experimental conditions, to inhibit yeast phosphofructokinase-1. In the absence of AMP and fructose-2,6-bisphosphate ADP increases the apparent affinity of the enzyme to fructose-6-phosphate. At low ATP concentrations the maximum activity with respect to fructose-6-phosphate decreases in the presence of ADP, while at high ATP a significant increase of the maximum activity by ADP is observed. In the presence of fructose-2,6-bisphosphate and AMP only the inhibiting effect of ADP persists. The data may be interpreted in terms of a hyperbolic inhibition mechanism.
Related Publications
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
June 1982,
FEBS letters,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
October 1981,
Biochemical and biophysical research communications,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
January 1984,
Development, growth & differentiation,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
December 1981,
Biochemical and biophysical research communications,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
April 1981,
The Journal of biological chemistry,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
January 1988,
Comparative biochemistry and physiology. B, Comparative biochemistry,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
June 1982,
FEBS letters,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
June 1983,
The Journal of biological chemistry,
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
March 1991,
Clinical science (London, England : 1979),
K Nissler, and
W Schellenberger, and
A Otto, and
E Hofmann
January 1985,
Biochemical and biophysical research communications,
