890531-64-3

Upstream product

• 890531-57-4 p-nitrophenyl 2-acetamido-2-deoxy-3,4-O-(2',3'-dimethoxybutane-2',3'-diyl)-β-D-glucopyranoside 
• 824-78-2 4-nitrophenol sodium salt 
• 3459-18-5 4-nitrophenyl N-acetyl-β-D-glucosaminide 
• 3068-34-6 Acetic acid (2R,3S,4R,5R,6R)-3-acetoxy-2-acetoxymethyl-5-acetylamino-6-chloro-tetrahydro-pyran-4-yl ester 

Downstream Products

• 890531-65-4 p-nitrophenyl 2-acetamido-2-deoxy-3,4-O-(2',3'-dimethoxybutane-2',3'-diyl)-β-D-glucopyranosiduronitrile 
• 890531-52-9 p-nitrophenyl 2-acetamido-2-deoxy-β-D-glucopyranosiduronitrile 

Relevant academic research and scientific papers

Cyanodeoxy-glycosyl derivatives as substrates for enzymatic reactions

Synthetic routes for the preparation of new sugar nitriles 8-10 derived from 2-acetamido-2-deoxy-β-D-glucopyranosides bearing a cyano group at the C-5 or C-6 position are presented. In an attempt to prepare the glycosyl azide 10 by treatment of tosylate 23 with KCN/DMF at 60°C, an intramolecular 1,3-dipolar cycloaddition reaction occurred to give the highly constrained nonisolable tetrazole 24, which was readily converted into the imino-azido compound 25 through an azido-tetrazole tautomerism. Compounds 8 and 10 were found to be poorer substrates of fungal β-N-acetylhexosaminidases than compound 9 and none of these compounds was accepted as substrates of the nitrilase or nitrile hydratase. Docking of the nitriles 8-10 in the active site of the β-N-acetylhexosaminidase from Aspergillus oryzae gave interaction energies comparable with the natural substrate. Based on these data, which indicate strong binding of these compounds (8 > 9 > 10) to the active site, it has been proposed that some cyano derivatives may act as competitive inhibitors of β-N-acetylhexosaminidases. This hypothesis is consistent with enzyme inhibition experiments which showed strong inhibitory properties of compound 9 (KI = 0.37 mM) and in particular of compound 8 (KI = 7.6 μM). Wiley-VCH Verlag GmbH & Co. KGaA, 2006.