Title

GlcNAc-Thiazoline Conformations

Document Type

Article

Publication Date

3-1-2009

Published In

Bioorganic And Medicinal Chemistry

Abstract

The title compound, a powerful inhibitor of retaining N-acetylhexosaminidases, can move freely among three pyranose solution conformations of similar energy-two twist boats and the (4)C(1) chair-as revealed by NMR, calculational, and crystallographic studies. It binds in the enzyme active site only in the pseudo-(4)C(1) conformation, however, in which it most closely resembles the hypothetical bound substrate transition state, a (4)E sofa that is approximately trigonal bipyramidal at the anomeric carbon. (C) 2009 Elsevier Ltd. All rights reserved.

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