895161-76-9

Upstream product

• 1125-88-8 benzaldehyde dimethyl acetal 
• 895161-74-7 4-pentenyl O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-(1->4)-3,6-di-O-acetyl-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 191545-14-9 2-methyl-4,5-dihydro-[4-O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-3,6-di-O-acetyl-1,2-dideoxy-α-D-glucopyranoso][2,1-d]-1,3-oxazole 
• 91878-42-1 2',3',4',6'-tetra-O-acetyl-β-D-glucopyranosyl-(1→4)-3,6-di-O-acetyl-2-azido-2-deoxy-1-O-nitro-β-D-glucopyranose 
• 36954-64-0 O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-(1->4)-2-acetamido-1,3,6-tri-O-acetyl-2-deoxy-α-D-glucopyranose 

Downstream Products

• 895161-80-5 4-pentenyl O-(3-O-benzoyl-4,6-O-benzylidene-β-D-glucopyranosyl)-(1->4)-3,6-di-O-benzoyl-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 895161-78-1 4-pentenyl O-(2,3-di-O-acetyl-4,6-O-benzylidene-β-D-glucopyranosyl)-(1->4)-3,6-di-O-acetyl-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 895161-89-4 4-pentenyl O-(2,3,4-O-triacetyl-6-O-benzyl-β-D-mannopyranosyl)-(1->4)-2-acetamido-3,6-di-O-acetyl-2-deoxy-β-D-glucopyranoside 
• 895161-66-7 C₂₁H₂₉NO₁₀ 
• 895161-82-7 4-pentenyl O-(2,3-di-O-benzoyl-4,6-O-benzylidene-β-D-mannopyranosyl)-(1->4)-3,6-di-O-benzoyl-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 895161-91-8 C₃₁H₃₉NO₁₅ 
• 895161-93-0 4-pentenyl O-(2,3-di-O-benzoyl-β-D-mannopyranosyl)-(1->4)-2-acetamido-3,6-di-O-benzoyl-2-deoxy-β-D-glucopyranoside 

Relevant academic research and scientific papers

GLYCOPROTEIN SYNTHESIS AND REMODELING BY ENZYMATIC TRANSGLYCOSYLATION

A chemoenzymatic method for the preparation of a homogeneous glycoprotein or glycopeptide, including (a) providing an acceptor selected from the group consisting of GlcNAc-protein and GlcNAc-peptide; and (b) reacting the acceptor with a donor substrate in

Glycopeptide synthesis through endo-glycosidase-catalyzed oligosaccharide transfer of sugar oxazolines: Probing substrate structural requirement

An array of sugar oxazolines was synthesized and tested as donor substrates for the Arthrobacter endo-ssN-acetylglucosaminidase (Endo-A)-catalyzed glycopeptide synthesis. The experiments revealed that the minimum structure of the donor substrate required for Endo-A catalyzed transglycosylation is a Manss1→4-GlcNAc oxazoline moiety. Replacement of the ss-D-Man moiety with ss-D-Glc, ss-D-Gal, and ss-D-GlcNAc monosaccharides resulted in the loss of substrate activity for the disaccharide oxazoline. Despite this, the enzyme could tolerate modifications such as attachment of additional sugar residues or a functional group at the 3- and/or 6-positions of the ss-D-Man moiety, thus allowing a successful transfer of selectively modified oligosaccharides to the peptide acceptor. On the other hand, the enzyme has a great flexibility for the acceptor portion and could take both small and large GlcNAc-peptides as the acceptor. The studies implicate a great potential of the endoglycosidase-catalyzed transglycosylation for constructing both natural and selectively modified glycopeptides.