The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose 1,6-bisphosphatase |
| |
Authors: | D.W. Meek H.G. Nimmo |
| |
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. |
| |
Keywords: | Fructose 1,6-bisphosphatase Fructose 2,6-bisphosphate N-Ethylmaleimide High substrate inhibition Allosteric site |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|