Determination of the solution conformation of D-gluco-dihydroacarbose, a high-affinity inhibitor bound to glucoamylase by transferred NOE NMR spectroscopy.

Abstract

The determination of the bound solution conformation of D-gluco-dihydroacarbose (GAC), a tight-binding inhibitor of several glycosidase and amylase enzymes, by glucoamylase is described. Transferred NOE NMR experiments and line-broadening effects indicate that GAC is bound in a conformation resembling that observed in the crystal structure. This contrasts… (More)

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Cite this paper

@article{Weimar2000DeterminationOT, title={Determination of the solution conformation of D-gluco-dihydroacarbose, a high-affinity inhibitor bound to glucoamylase by transferred NOE NMR spectroscopy.}, author={Timo Weimar and Bjorn Petersen and Birte Svensson and B. Pinto}, journal={Carbohydrate research}, year={2000}, volume={326 1}, pages={50-5} }