568586-70-9

Upstream product

• 108-24-7 acetic anhydride 
• 2106-10-7 1-deoxy-1-fluoro-α-D-glucose 
• 568586-63-0 (3R,4R,5R)-N-benzyloxycarbonyl-3,4-dihydroxy-5-(hydroxymethyl)piperidine 
• 1333317-40-0 (3R,4R,5R)-3-acetoxy-N-benzyloxycarbonyl-4-hydroxy-5-(hydroxymethyl)piperidine 
• 1333317-41-1 (3R,4R,5R)-3-acetoxy-5-acetyloxymethyl-N-benzyloxycarbonyl-4-hydroxypiperidine 
• 153765-53-8 C₄₀H₅₂Cl₃NO₂₆ 
• 501-53-1 benzyl chloroformate 
• 169105-89-9 isofagomine 

Relevant academic research and scientific papers

A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine

Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using thes

Synthesis with glycosynthases: Cello-oligomers of isofagomine and a tetrahydrooxazine as cellulase inhibitors

Isofagomine and a carbohydrate-like tetrahydrooxazine, as their N-benzyloxycarbonyl derivatives, have been subjected to a glycosynthase in the presence of α-D-glucopyranosyl fluoride as a glucosyl donor. In each case, after protecting group removal, a mixture of 1,4-β-linked di-, tri-, and tetra-'saccharides' was obtained. These novel oligosaccharide derivatives were tested as inhibitors of the endo-glycanase Cex from Cellulomonas fimi. Affinities increased progressively as additional D-glucosyl residues were incorporated, which is consistent with the known substrate specificity of this enzyme.