42868-96-2

Basic information

• Product Name: 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl bromide
• Synonyms: 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl bromide
• CAS NO: 42868-96-2
• Molecular Weight: 525.353
• Mol File: 42868-96-2.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl bromide(CAS DataBase Reference)
• NIST Chemistry Reference: 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl bromide(42868-96-2)
• EPA Substance Registry System: 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl bromide(42868-96-2)

Safety Data

• Hazardous Substances Data: 42868-96-2(Hazardous Substances Data)

Upstream product

• 98-88-4 benzoyl chloride 
• 189074-35-9 1-O-Acetyl-2,3,5-tri-O-benzoyl-α/β-L-arabinofuranoside 
• 42793-97-5 2,3,5-tri-O-benzoyl-1-O-methyl-α-L-arabinofuranose 
• 3795-68-4 methyl α-L-arabinofuranoside 
• 22796-65-2 p-nitrophenyl α-L-arabinofuranoside 
• 5328-37-0 L-arabinose 

Downstream Products

• 97424-66-3 2-((2R,3R,4S,5S)-3,4-Bis-benzoyloxy-5-benzoyloxymethyl-tetrahydro-furan-2-yl)-4-bromo-isoquinolinium; bromide 
• 133008-03-4 1,2-Di-O-acetyl-3,5-di-O-benzoyl-L-arabinofuranose 
• 1258598-77-4 2,3,5-tribenzoyl-α-L-arabinofuranosyl azide 
• 1190749-50-8 phenyl 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl-(1->3)-6-O-acetyl-2,4-di-O-benzoyl-β-D-galactopyranosyl-(1->6)-2,3,4-tri-O-benzoyl-1-thio-β-D-galactopyranoside 
• 1190749-44-0 3-azidopropyl 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl-(1->3)-6-O-acetyl-2,4-di-O-benzoyl-β-D-galactopyranosyl-(1->6)-2,3,4-tri-O-benzoyl-β-D-galactopyranoside 
• 113575-02-3 1,2--α-D-ribofuranose 
• 77164-48-8 α-L-arabinofuranosylmethyl-(p-nitrophenyl)triazene 
• 77471-44-4 7-hydroxy-4-methylcoumarin-7-yl α-L-arabinofuranoside 
• 192223-19-1 2,3,4-tri-O-benzyl-3-O-(2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl)-β-D-galactopyranosyl chloride 
• 290820-41-6 8'-phthalimidooctyl 2,3,5-tri-O-benzoyl-α-L-arabinofuranoside 
• 243869-84-3 Methyl 2,4-do-O-benzyl-3-O-(2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl)-β-D-xylopyranoside 
• 249511-76-0 2,3,5-tri-O-benzoyl-α-L-arabinofuranosyl-(1-> 6)-3,4-O-isopropylidene-β-D-galactopyranosyl-(1-> 6)-1,2:3,4-di-O-isopropylidene-α-D-galactopyranose 

Relevant articles and documents

Active Site Mapping of Xylan-Deconstructing Enzymes with Arabinoxylan Oligosaccharides Produced by Automated Glycan Assembly

Xylan-degrading enzymes are crucial for the deconstruction of hemicellulosic biomass, making the hydrolysis products available for various industrial applications such as the production of biofuel. To determine the substrate specificities of these enzymes, we prepared a collection of complex xylan oligosaccharides by automated glycan assembly. Seven differentially protected building blocks provided the basis for the modular assembly of 2-substituted, 3-substituted, and 2-/3-substituted arabino- and glucuronoxylan oligosaccharides. Elongation of the xylan backbone relied on iterative additions of C4-fluorenylmethoxylcarbonyl (Fmoc) protected xylose building blocks to a linker-functionalized resin. Arabinofuranose and glucuronic acid residues have been selectively attached to the backbone using fully orthogonal 2-(methyl)naphthyl (Nap) and 2-(azidomethyl)benzoyl (Azmb) protecting groups at the C2 and C3 hydroxyls of the xylose building blocks. The arabinoxylan oligosaccharides are excellent tools to map the active site of glycosyl hydrolases involved in xylan deconstruction. The substrate specificities of several xylanases and arabinofuranosidases were determined by analyzing the digestion products after incubation of the oligosaccharides with glycosyl hydrolases.

Araf51 with improved transglycosylation activities: One engineered biocatalyst for one specific acceptor

A random mutagenesis of the arabinofuranosyl hydrolase Araf51 has been run in order to have access to efficient biocatalysts for the synthesis of alkyl arabinofuranosides. The mutants were selected on their ability to catalyze the transglycosylation reaction of p-nitrophenyl α-l-arabinofuranoside (pNP-Araf) used as a donor and various aliphatic alcohols as acceptors. This screening strategy underlined 5 interesting clones, each one corresponding to one acceptor. They appeared to be much more efficient in the transglycosylation reaction compared to the wild type enzyme whereas no self-condensation or hydrolysis products could be detected. Moreover, the high specificity of the mutants toward the alcohols for which they have been selected validates the screening process. Sequence analysis of the mutated enzymes revealed that, despite their location far from the active site, the mutations affect significantly the kinetics properties as well as the substrate affinity of these mutants toward the alcohol acceptors in the transglycosylation reaction.