AbstractFructose 2,6-bisphosphate has been claimed to be both a substrate analogue and an allosteric inhibitor of fructose-1,6-bisphosphatase. The results reported here show that fructose 2,6-bisphosphate can be both an inhibitor and an activator of the enzyme, depending on the substrate concentration. This biphasic behaviour at saturating concentrations of substrate can only be due to an allosteric effect. In addition to the mechanistic implication it is possible that this finding may have physiological meaning
Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis. In mammals,...
AbstractThe effect of fructose 2,6-bisphosphate on the dynamics of the 6-phosphofructo-1-kinase/fruc...
Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleim...
AbstractFructose 2,6-bisphosphate has been claimed to be both a substrate analogue and an allosteric...
AbstractRat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-eth...
AbstractRat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated in...
Fructose 1,6-bisphosphatase has been isolated from rat liver by a newly developed procedure which in...
The fructose 1,6-bisphosphatase (FBPase) reaction was investigated in the reverse direction by using...
The effect of thiol group modification of rabbit liver fructose-1,6-bisphosphatase by N-ethylmaleimi...
Fructose 1,6-bisphosphatase has been isolated from rat liver by a newly developed procedure which in...
Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. It is a potential drug targ...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
AbstractRat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-eth...
Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis. In mammals,...
AbstractThe effect of fructose 2,6-bisphosphate on the dynamics of the 6-phosphofructo-1-kinase/fruc...
Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleim...
AbstractFructose 2,6-bisphosphate has been claimed to be both a substrate analogue and an allosteric...
AbstractRat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-eth...
AbstractRat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated in...
Fructose 1,6-bisphosphatase has been isolated from rat liver by a newly developed procedure which in...
The fructose 1,6-bisphosphatase (FBPase) reaction was investigated in the reverse direction by using...
The effect of thiol group modification of rabbit liver fructose-1,6-bisphosphatase by N-ethylmaleimi...
Fructose 1,6-bisphosphatase has been isolated from rat liver by a newly developed procedure which in...
Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. It is a potential drug targ...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
Inhibition of rat liver fructose-1,6-bisphosphatase by AMP was uncompetitive with respect to fructos...
AbstractRat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-eth...
Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis. In mammals,...
AbstractThe effect of fructose 2,6-bisphosphate on the dynamics of the 6-phosphofructo-1-kinase/fruc...
Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleim...