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Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase
F Orosz1, T Y Christova, J Ovádi
1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest.
Biochemical and Biophysical Research Communications
|September 30, 1987
Abstract:
The effect of aldolase on the concentration-dependent kinetic behaviour of phosphofructokinase was investigated by means of covalently attached fluorescent probe and by using a kinetic approach. The dimeric form of kinase in equilibrium with the active tetramer interacts with the native aldolase with an apparent dissociation constant of 2.5 microM. Within this heterologous enzyme complex the phosphofructokinase is catalytically active probably because the aldolase binding to nascent kinase dimers might protect them against inactivation.