Allosteric inhibition of Dictyostelium discoideum fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate

It has been found that the inhibition of Dictyostelium discoideum fructose-1,6-bisphosphatase by fructose 2,6-P 2 greatly diminished when the pH was raised to the range 8.5–9.5, which resulted in a marked decrease of the affinity for the inhibitor with no change in the K m for the substrate. This pr...

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Bibliographic Details
Published in:FEBS letters 1988-12, Vol.241 (1), p.51-54
Main Authors: ANDRES, V, GARCIA-SALGUERO, L, GOMEZ, M.-E, ARAGON, J. J
Format: Article
Language:English
Subjects:
Allosteric Regulation
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Dictyostelium - enzymology
Dictyostelium discoideum
Enzymes and enzyme inhibitors
Fructose 2,6-bisphosphate
Fructose-1,6-bisphosphatase
Fructose-Bisphosphatase - antagonists & inhibitors
Fructosediphosphates - pharmacology
Fundamental and applied biological sciences. Psychology
Hexosediphosphates - pharmacology
Hydrolases
Kinetics
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Summary:It has been found that the inhibition of Dictyostelium discoideum fructose-1,6-bisphosphatase by fructose 2,6-P 2 greatly diminished when the pH was raised to the range 8.5–9.5, which resulted in a marked decrease of the affinity for the inhibitor with no change in the K m for the substrate. This provides evidence for the involvement of an allosteric site for fructose 2,6-P 2. Moreover, the fact that excess substrate inhibition also decreased at the pH values for minimal fructose 2,6-P 2 inhibition, and was essentially abolished in the presence of fructose 2,6-P 2, strongly suggests that this inhibition takes place by binding of fructose 1,6-P 2 as a weak analogue of the physiological effector fructose 2,6-P 2.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)81029-9