Inhibition of Escherichia coli fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate
Autor: | Frank Marcus, Judith Rittenhouse, Ida Edelstein |
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Rok vydání: | 1984 |
Předmět: |
Biophysics
Fructose 1 6-bisphosphatase medicine.disease_cause Biochemistry Phosphoenolpyruvate chemistry.chemical_compound Escherichia coli Fructosediphosphates medicine Molecular Biology chemistry.chemical_classification biology Chemistry Active site Fructose Cell Biology Substrate concentration Adenosine Monophosphate Fructose-Bisphosphatase Kinetics Enzyme Fructose 2 6-bisphosphate biology.protein Hexosediphosphates Phosphoenolpyruvate carboxykinase |
Zdroj: | Biochemical and Biophysical Research Communications. 119:1103-1108 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(84)90888-x |
Popis: | Fructose 2,6-bisphosphate, a potent inhibitor of fructose-1,6-bisphosphatases, was found to be an inhibitor of the Escherichia coli enzyme. The substrate saturation curves in the presence of inhibitor were sigmoidal and the inhibition was much stronger at low than at high substrate concentrations. At a substrate concentration of 20 μM, 50% inhibition was observed at 4.8 μM fructose 2,6-bisphosphate. Escherichia coli fructose-1,6-bisphosphatase was inhibited by AMP (Kj = 16 μM) and phosphoenolpyruvate caused release of AMP inhibition. However, neither AMP inhibition nor its release by phosphoenolpyruvate was affected by the presence of fructose 2,6-bisphosphate. The results obtained, together with previous observations, provide further evidence for the fructose 2,6-bisphosphate-fructose-1,6-bisphosphatase active site interaction. |
Databáze: | OpenAIRE |
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