489-52-1

Basic information

• Product Name: 2-ACETAMIDO-2-DEOXY-3-O-(BETA-D-GALACTOPYRANOSYL)-D-GLUCOPYRANOSE
• Synonyms: D-Glucopyranose, 2-(acetylamino)-2-deoxy-3-O-β-D-galactopyranosyl-
• CAS NO: 489-52-1
• Molecular Formula: C₁₄H₂₅NO₁₁
• Molecular Weight: 383.348
• Mol File: 489-52-1.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 2-ACETAMIDO-2-DEOXY-3-O-(BETA-D-GALACTOPYRANOSYL)-D-GLUCOPYRANOSE(CAS DataBase Reference)
• NIST Chemistry Reference: 2-ACETAMIDO-2-DEOXY-3-O-(BETA-D-GALACTOPYRANOSYL)-D-GLUCOPYRANOSE(489-52-1)
• EPA Substance Registry System: 2-ACETAMIDO-2-DEOXY-3-O-(BETA-D-GALACTOPYRANOSYL)-D-GLUCOPYRANOSE(489-52-1)

Safety Data

• Hazardous Substances Data: 489-52-1(Hazardous Substances Data)

Usage

Structure

Hexosamine sugar molecule

Function

Component of glycoproteins, glycolipids, and proteoglycans in the body

Role

Important component of A, B, and O blood group antigens

Biological functions

Cell-cell recognition, adhesion, inflammation, immune response, cancer progression

Applications

Synthesis of pharmaceuticals and research tools

Unique chemical properties

Make it useful in various applications and studies

Upstream product

• 57467-13-7 4-nitrophenyl (O-β-D-galactopyranosyl)-(1-3)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 3150-24-1 4-nitrophenyl-β-D-galactopyranoside 

Downstream Products

• 57467-13-7 4-nitrophenyl (O-β-D-galactopyranosyl)-(1-3)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 710306-57-3 4-nitrophenyl 2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 142434-22-8 O-(5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic-acid)-(2-3)-O-β-D-galactopyranosyl-(1-3)-2-acetamido-2-deoxy-β-D-glucopyranose 
• 142434-21-7 O-(5-acetamido-3,5-dideoxy-α-D-glycero-D-galacto-2-nonulopyranosylonic-acid)-(2-3)-O-β-D-galactopyranosyl-(1-3)-2-acetamido-2-deoxy-α-D-glucopyranose 
• 1314876-73-7 α-D-mannopyranosyl-(1->3)-2-amino-1,2-deoxy-1-(2-triphenylmethylthioeth-2-ylamino)-D-glucitol 

Relevant articles and documents

Novel substrate specificities of two lacto-N-biosidases towards β-linked galacto-N-biose-containing oligosaccharides of globo H, Gb5, and GA1

We describe the novel substrate specificities of two independently evolved lacto-N-biosidases (LnbX and LnbB) towards the sugar chains of globo- and ganglio-series glycosphingolipids. LnbX, a non-classified member of the glycoside hydrolase family, isolated from Bifidobacterium longum subsp. longum, was shown to liberate galacto-N-biose (GNB: Galβ1-3GalNAc) and 2′-fucosyl GNB (a type-4 trisaccharide) from Gb5 pentasaccharide and globo H hexasaccharide, respectively. LnbB, a member of the glycoside hydrolase family 20 isolated from Bifidobacterium bifidum, was shown to release GNB from Gb5 and GA1 oligosaccharides. This is the first report describing enzymatic release of β-linked GNB from natural substrates. These unique activities may play a role in modulating the microbial composition in the gut ecosystem, and may serve as new tools for elucidating the functions of sugar chains of glycosphingolipids.

Highly efficient and regioselective enzymatic synthesis of β-(1→3) galactosides in biosolvents

A green synthesis for β-(1→3) galactosyldisaccharides that combines the use of a biodegradable biocatalyst, aqueous solutions, and solvent recycling (renewable and derived from biomass) has been developed. The use of biomass-derived solvents allows good catalytic activity in the synthesis of Gal-β-d-(1→3)GlcNAc and Gal-β-d-(1→)3GalNAc (99% and 95% yields respectively) with β-Gal-3-NTag β-galactosidase, preventing hydrolytic activity and with full regioselectivity. This represents a considerable improvement over the use of an aqueous buffer or conventional organic solvents. Furthermore, reaction scaling up and biosolvent recycling are feasible without losing catalytic action. In order to understand the role of these green solvents in the enzyme's synthetic behaviour, different structural studies were performed (fluorescence and molecular modelling) in the presence of some selected biosolvents to conclude that the presence of green biosolvents in the reaction media modifies the enzyme's tertiary structure allowing better substrate disposition in the active site, most probably due to solvation effects, explaining the behaviour observed. The Royal Society of Chemistry 2013.