269065-36-3

Upstream product

• 98-88-4 benzoyl chloride 
• 6082-04-8 methyl 2-acetylamido-2-deoxy-D-glucoside 
• 95245-35-5 methyl 2-acetamido-3-O-benzoyl-2-deoxy-α-D-glucopyranoside 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 3055-46-7 methyl N-acetyl-D-glucosamine 
• 6619-04-1 N-((4aR,6S,7R,8R,8aS)-8-Hydroxy-6-methoxy-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-7-yl)-acetamide 

Downstream Products

• 269065-37-4 methyl 2-acetamido-3,6-di-O-benzoyl-2,4-dideoxy-α-D-xylo-hexopyranoside 
• 176691-03-5 methyl 2-acetamido-3,6-di-O-benzoyl-2-deoxy-4-O-trifluoromethanesulfonyl-β-D-galactopyranoside 
• 666848-65-3 methyl 4,6-di-O-acetyl-2,3-di-O-benzoyl-α-D-mannopyranosyl-(1-> 4)-2-acetamido-3,6-di-O-benzoyl-2-deoxy-α-D-glucopyranoside 
• 77870-70-3 methyl 2-acetamido-3,6-di-O-acetyl-2,4-dideoxy-4-fluoro-α-D-glucopyranoside 
• 176691-02-4 methyl 2-acetamido-3,6-di-O-benzoyl-2-deoxy-α-D-galactopyranoside 
• 290819-64-6 methyl 2-acetamido-3,6-di-O-benzoyl-2,4-dideoxy-4-fluoro-α-D-glucopyranoside 
• 1370586-83-6 methyl 2-acetamido-3,6-di-O-benzoyl-2-deoxy-α-D-xylo-hexapyranosid-4-ulose 

Relevant academic research and scientific papers

Inhibition of microbial β-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline

NAG-thiazoline is a well-established competitive inhibitor of two physiologically relevant glycosidase families - β-N-acetylhexosaminidases (GH20) and β-N-acetylglucosaminidases (GH84). Based on the different substrate flexibilities of these enzyme groups, we designed and synthesized the 4-deoxy derivative of NAG-thiazoline aiming at the selective inhibition of GH20 β-N-acetylhexosaminidases. One GH84 and two GH20 microbial glycosidases were employed as model enzymes for the inhibition assays. Surprisingly, the new compound 4-deoxy-thiazoline exhibited no activity inhibition with either of the enzyme families of interest. Unlike with the substrates, the 4-hydroxyl group of the inhibitor's sugar ring seems to be crucial for binding the inhibitor to the active sites of these enzymes.

3- and 4-uloses derived from N-acetyl- D -glucosamine: A unique pair of complementary organocatalysts for asymmetric epoxidation of alkenes

The 4-ulose and the 3-ulose, both derived in two steps from the α-methyl glycoside of N-acetyl-D-glucosamine (GlcNAc), act as organocatalysts in the asymmetric epoxidation of alkenes, with unprecedented complementary enantioselectivity. The best results are found with α,β-unsaturated esters as substrates, with enantiomeric ratios up to 90:10 and 11:89, respectively. Copyright

Synthesis of two oligosaccharides, the GPI anchor glycans from S. cerevesiae and A. fumigatus

Two oligosaccharides, α-D-Manp-(1→2)-α-D-Manp-(1→2)- α-D-Manp-(1→6)-α-D-Manp-(1→4)-α-D-GlcpNAc (I) and α-D-Manp-(1→3)-α-D-Manp-(1→2)-α-D-Manp-(1→2) -α-D-Manp-(1→6)-α-D-Manp-(1→4)-α-D-GlcpNAc (II), the glycosylphosphatidylinositol (GPI) anchor glycans from

Synthesis of 4-deoxy analogues of 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-xylose and their effects on glycoconjugate biosynthesis

4-Deoxy analogues of 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-xylose were synthesized and evaluated as inhibitors of glycoconjugate biosynthesis. Methyl 2-acetamido-2,4-dideoxy-β-D-xylo-hexopyranoside (11) showed a reduction in [3/sup

Synthesis of 4-deoxy-4-fluoro analogues of 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-galactose and their effects on cellular glycosaminoglycan biosynthesis

4-Deoxy-4-fluoro analogues of 2-acetamido-2-deoxy-D-glucose and 2-acetamido-2-deoxy-D-galactose were synthesized and evaluated as inhibitors of hepatic glycosaminoglycan biosynthesis. 2-Acetamido-1,3,6-tri-O-acetyl-2,4-dideoxy-4-fluoro-D-glucopyranose (16) exhibited a reduction of [3H]GlcN and [35S]SO4 incorporation into hepatocyte cellular glycosaminoglycans to 12 and 18%, respectively, of the control cells, at 1.0 mM. Similarly, 2-acetamido-1,3,6-tri-O-acetyl-2,4-dideoxy-4-fluoro-D-galactopyranose (31) exhibited a reduction of [3H]GlcN and [35S]SO4 incorporation to 1 and 9%, respectively, of the control cells, at 1.0 mM. Unlike 16, 31 exhibited a reduction of [14C]Leu incorporation into cellular protein to 57% of control cells, at 1.0 mM. Copyright (C) 2000 Elsevier Science Ltd.