GlcNAc-Thiazoline conformations.
Bioorg Med Chem
; 17(5): 1831-6, 2009 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-19223181
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Tiazóis
/
Glucosamina
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article