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.
Recommended Citation
S. Knapp, D. Fash, M. Abdo, T. J. Emge, and Paul R. Rablen.
(2009).
"GlcNAc-Thiazoline Conformations".
Bioorganic And Medicinal Chemistry.
Volume 17,
Issue 5.
1831-1836.
DOI: 10.1016/j.bmc.2009.01.066
https://works.swarthmore.edu/fac-chemistry/85
