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

FEBS Letters

Meek, D.W.¹  Nimmo, H.G.¹ 

[1] Department of Biochemistry, University of Glasgow, Glasgow G12 8QQ, Scotland

关键词: Fructose 1;    6-bisphosphatase;    Fructose 2;    6-bisphosphate;    N-Ethylmaleimide;    High substrate inhibition;    Allosteric site;   

DOI  :  10.1016/0014-5793(83)80946-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown