Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate.
Journal of Biological ChemistryPublished 1 April 1981Open access
S.J. Pilkis, M. Raafat El‐Maghrabi, J Pilkis, T.H. Claus
Citations236
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SJR score1.71
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TL;DR
Rat liver fructose-1,6-bisph phosphatase, which was assayed by measuring the release of 32P from fructose 1,6-[1-32P]bisphosphate at pH 7.5, exhibited hyperbolic kinetics with regard to its substrate.
Abstract
Rat liver fructose-1,6-bisphosphatase, which was assayed by measuring the release of 32P from fructose 1,6-[1-32P]bisphosphate at pH 7.5, exhibited hyperbolic kinetics with regard to its substrate. beta-D-Fructose 2,6-bisphosphate, an activator of hepatic phosphofructokinase, was found to be a potent inhibitor of the enzyme. The inhibition was competitive in nature and the Ki was estimated to be 0.5 microM. The Hill coefficient for the reaction was 1.0 in the presence and absence of fructose 2,6-bisphosphate. Fructose 2,6-bisphosphate also enhanced inhibition of the enzyme by the allosteric inhibitor AMP. The possible role of fructose 2,6-bisphosphate in the regulation of substrate cycling at the fructose-1,6-bisphosphatase step is discussed.
Keywords
Biochemistry, Genetics and Molecular Biology
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