| Autor: |
Palcic MM; Department of Chemistry, University of Alberta, Edmonton, Canada. monica.palcic@ualberta.ca, Scaman CH, Otter A, Szpacenko A, Romaniouk A, Li YX, Vijay IK |
| Jazyk: |
angličtina |
| Zdroj: |
Glycoconjugate journal [Glycoconj J] 1999 Jul; Vol. 16 (7), pp. 351-5. |
| DOI: |
10.1023/a:1007096011392 |
| Abstrakt: |
Alpha-glucosidase I is a key enzyme in the biosynthesis of asparagine-linked oligosaccharides catalyzing the first processing event after the en bloc transfer of Glc3Man9GlcNAc2 to proteins. This enzyme is an inhibitor target for anti-viral agents that interfere with the formation of essential glycoproteins required in viral assembly, secretion and infectivity. Of fundamental mechanistic interest for all oligosaccharide hydrolyzing enzymes is the stereochemical course of the reaction which can occur with either retention or inversion of anomeric configuration. The stereochemistry is used to categorize enzymes and is important in designing mechanism-based inhibitors. To determine the stereochemical course of the alpha-glucosidase I reaction, the release of glucose from a synthetic trisaccharide substrate, Glc(alpha1-2)Glc(alpha1-3)Glc alphaO(CH2)8COOCH3 was directly monitored by 1H NMR spectroscopy. Both the yeast and bovine mammary gland enzymes released beta-glucose concomitant with the formation of the Glc(alpha1-3)Glc alphaO(CH2)8COOCH3 disaccharide product demonstrating that both enzymes operate with inversion of anomeric configuration. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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