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Allosteric inhibition of Dictyostelium discoideum fructose‐1,6‐bisphosphatase by fructose 2,6‐bisphosphate
Author(s) -
Andrés Vicente,
García-Salguero Leticia,
Gómez María-Esther,
Aragón Juan J.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81029-9
Subject(s) - dictyostelium discoideum , allosteric regulation , fructose , fructose 1,6 bisphosphatase , fructose 2,6 bisphosphate , chemistry , biochemistry , substrate (aquarium) , enzyme , biology , glycolysis , phosphofructokinase , ecology , gene
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 .