136520-23-5

Upstream product

• 54400-75-8 allyl 2-acetamido-2-deoxy-β-D-glucopyranoside 
• 2186-92-7 p-Anisaldehyde dimethyl acetal 
• 54400-75-8 allyl 2-acetamido-2-deoxy-α-D-glucopyranoside 
• 123-11-5 4-methoxy-benzaldehyde 

Downstream Products

• 136882-25-2 allyl 2-acetamido-2-deoxy-3-O-(methoxycarbonyl)-4,6-O-(p-methoxybenzylidene)-β-D-glucopyranoside 
• 1092840-25-9 allyl 2-acetamido-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-2-deoxy-4,6-O-p-methoxybenzylidene-β-D-glucopyranoside 
• 1314876-68-0 allyl 2-acetamido-2-deoxy-3-O-levulinoyl-4,6-O-p-methoxybenzylidene-β-D-glucopyranoside 
• 136408-99-6 2-Acetamido-2,4-didesoxy-6-O-(4-methoxybenzyl)-3-O-(methoxymethyl)-D-xylo-hexopyranose-oxim-O-methylether 
• 136408-88-3 Allyl-2-acetamido-3-O-acetyl-2-desoxy-6-O-(4-methoxybenzyl)-4-O-(trifluormethylsulfonyl)-α-D-glucopyranosid 
• 136409-05-7 5-O-Benzyl-2-(N-benzylacetamido)-6-O-(4-methoxybenzyl)-D-erythro-hex-3-enopyranose-oxim-O-methylether 
• 136408-87-2 Allyl-2-acetamido-3-O-acetyl-2-desoxy-6-O-(4-methoxybenzyl)-4-O-(methylsulfonyl)-α-D-glucopyranosid 
• 136408-83-8 Allyl-2-acetamido-3-O-benzoyl-2-desoxy-6-O-(4-methoxybenzyl)-α-D-glucopyranosid 
• 136408-93-0 Allyl-2-acetamido-2-desoxy-6-O-(4-methoxybenzyl)-3-O-(methoxymethyl)-4-O<(methylthio)thiocarbonyl>-α-D-glucopyranosid 
• 136409-06-8 2-Acetamido-2-desoxy-5-O-benzyl-6-O-(4-methoxybenzyl)-3-O-(methoxymethyl)-D-xylo-hexose-oxim-O-methylether 
• 136408-86-1 Allyl-2-acetamido-3-O-benzyl-2-desoxy-6-O-(4-methoxybenzyl)-α-D-glucopyranosid 
• 136408-89-4 Allyl-2-acetamido-3-O-acetyl-4-chlor-2,4-didesoxy-6-O-(4-methoxybenzyl)-α-D-galactopyranosid 
• 136408-82-7 Allyl-2-acetamido-3-O-acetyl-2-desoxy-6-O-(4-methoxybenzyl)-α-D-glucopyranosid 
• 136408-90-7 Allyl-2-acetamido-3-O-acetyl-2,4-didesoxy-6-O-(4-methoxybenzyl)-α-D-xylo-hexopyranosid 

Relevant academic research and scientific papers

Synthesis of a mannose-bearing disaccharide with a thiol spacer at the reducing end

The synthesis of a mannose-bearing disaccharide containing a thiol spacer at the reducing end was carried out to provide a tethered sugar suitable for attaching to gold nanoparticles. An array of such sugars is designed to mimic carbohydrates involved in cell-surface interactions. The molecule was constructed via Schmidt glycosylation of an appropriately protected glycosyl donor and an acceptor, followed by removal of protective groups and reductive amination to introduce a protected thiol spacer at the reducing end of the glycan. A new finding that the anomeric reductive amination is capable of concomitantly removing a neighboring N-acetyl group was also observed. Subsequent removal of the thiol protective group and purification of the product gave the target disaccharide in a satisfactory yield.

Oxime Derivatives of 2-Acetamido-2,4-dideoxy-D-xylo-hexose and of the Corresponding Uronic Acid

Oximes and O-methyl oximes of 3-O-protected 2-acetamido-2,4-dideoxy-D-xylo-hexose and of methyl 2-acetamido-2,4-dideoxy-D-xylo-hexuronate (14, 15, 16, 18, 19 and 26) have been prepared from 2-acetamido-2-deoxy-D-glucopyranose.Their structures have been el

Probing the Acceptor Specificity of β-1,4-Galactosyltransferase for the Development of Enzymatic Synthesis of Novel Oligosaccharides

β-1,4-Galactosyltransferase has been investigated with regard to its acceptor specificity and used in the synthesis of galactosides with 5-thioglucose, glucal, deoxynojirimycin, modified N-acetylglucosamine, and glucose derivatives as acceptors. The galactoside products are potentially useful as endoglycosidase or glycosyltransferase inhibitors or as intermediates for the synthesis of complex oligosaccharides. The conformation of each enzyme product has been investigated with NMR; all arc shown to possess similar glycosidic torsional angles based on a significant NOE between H-1 of Gal and H-4 of the acceptor. Comparison of the transferase reactions with the β-1,4-galactosidase-catalyzed galactosyl transfer reactions indicates that the transferase reactions provide exclusively a β-1,4-glycosidic linkage while the galactosidase reactions predominantly form a β-1,6-glycosidic linkage.