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Ribose 1,5-bisphosphate regulates rat kidney cortex phosphofructokinase.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology (2000-01-13)
T Ozeki, Y Mitsui, H Sugiya, S Furuyama
ABSTRACT

Phosphofructokinase (EC 2.7.1.11) is a major enzyme of the glycolytic pathway, catalyzing the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate. In this study, we demonstrated the effect of ribose 1,5-bisphosphate on phosphofructokinase purified from rat kidney cortex. Ribose 1,5-bisphosphate relieved the phosphofructokinase from ATP inhibition and increased the affinity for fructose 6-phosphate at nanomolar concentrations. These activating effects of ribose 1,5-bisphosphate were enhanced in the presence of AMP. Ribose 1,5-bisphosphate reduced the inhibition of the phosphofructokinase induced by citrate. These results suggest that ribose 1,5-bisphosphate is an activator of rat kidney cortex phosphofructokinase and synergistically regulates the enzyme activity with AMP.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
D-Ribulose 1,5-bisphosphate sodium salt hydrate, ≥90%
Sigma-Aldrich
D-Ribulose 1,5-bisphosphate sodium salt hydrate, ≥99.0% (TLC)