The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase

Meek, D.W. and Nimmo, H.G. (1983) The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase. FEBS Letters, 160(1-2), pp. 105-109. (doi: 10.1016/0014-5793(83)80946-6) (PMID:6309560)

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Abstract

Rat liver fructose 1,6‐bisphosphatase can be protected against partial inactivation by N‐ethylmaleimide by low concentrations of fructose 2,6‐bisphosphate or high concentrations of fructose 1,6‐bisphosphate. The partially inactivated enzyme has a much reduced sensitivity to high substrate inhibition and has lost the sigmoid component of the inhibition by fructose 2,6‐bisphosphate; this compound is a simple linear competitive inhibitor of the modified enzyme. The results suggest that fructose 2,6‐bisphosphate can bind to the enzyme at two distinct sites, the catalytic site and an allosteric site. High levels of fructose 1,6‐bisphosphate probably inhibit by binding to the allosteric site.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Meek, D.W., and Nimmo, H.G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:FEBS Letters
Publisher:FEBS
ISSN:0014-5793
ISSN (Online):1873-3468

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