Feed-forward activation and feed-back inhibition of pyruvate kinase type L of rat liver
T Tanaka, F Sue, H Morimura - Biochemical and biophysical research …, 1967 - Elsevier
T Tanaka, F Sue, H Morimura
Biochemical and biophysical research communications, 1967•ElsevierCrystalline type L pyruvate kinase was activated by fructose-1, 6-diphosphate. The Michaelis
constant for phosphoenolpyruvic acid decreased to about one tenth and the maximum
velocity was doubled by the presence of fructose-1, 6-diphosphate. The activity of type M
pyruvate kinase was not influenced significantly by fructose-1, 6-diphosphate. The sensitivity
to ATP inhibition of type L enzyme was decreased very markedly by fructose-1, 6-
diphosphate. Liver type L enzyme became completely insensitive to fructose-1, 6 …
constant for phosphoenolpyruvic acid decreased to about one tenth and the maximum
velocity was doubled by the presence of fructose-1, 6-diphosphate. The activity of type M
pyruvate kinase was not influenced significantly by fructose-1, 6-diphosphate. The sensitivity
to ATP inhibition of type L enzyme was decreased very markedly by fructose-1, 6-
diphosphate. Liver type L enzyme became completely insensitive to fructose-1, 6 …
Abstract
Crystalline type L pyruvate kinase was activated by fructose-1,6-diphosphate. The Michaelis constant for phosphoenolpyruvic acid decreased to about one tenth and the maximum velocity was doubled by the presence of fructose-1,6-diphosphate. The activity of type M pyruvate kinase was not influenced significantly by fructose-1,6-diphosphate. The sensitivity to ATP inhibition of type L enzyme was decreased very markedly by fructose-1,6-diphosphate. Liver type L enzyme became completely insensitive to fructose-1,6-diphosphate activation after 120 minutes incubation at low concentration at 37°C.
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