Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: kinetic and crystallographic studies.

Abstract

In an attempt to identify a new lead molecule that would enable the design of inhibitors with enhanced affinity for glycogen phosphorylase (GP), beta-D-glucopyranosyl bismethoxyphosphoramidate (phosphoramidate), a glucosyl phosphate analogue, was tested for inhibition of the enzyme. Kinetic experiments showed that the compound was a weak competitive… (More)

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Cite this paper

@article{Chrysina2005BindingOB, title={Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: kinetic and crystallographic studies.}, author={Evangelia D Chrysina and Magda N Kosmopoulou and Rozina Kardakaris and Nicolas Bischler and Demetres D Leonidas and Thanukrishnan Kannan and Duraikkannu Loganathan and Nikos G. Oikonomakos}, journal={Bioorganic & medicinal chemistry}, year={2005}, volume={13 3}, pages={765-72} }