7115-19-7

Basic information

• Product Name: Methyla-D-laminarabioside
• Synonyms: Methyla-D-laminarabioside
• CAS NO: 7115-19-7
• Molecular Formula: C₁₃H₂₄O₁₁
• Molecular Weight: 356.322
• Product Categories: Oligosaccharides
• Mol File: 7115-19-7.mol
• Article Data: 21

Chemical Properties

• Melting Point: 180-181°C
• Boiling Point: 669.2±55.0 °C(Predicted)
• Appearance: /
• Density: 1.63±0.1 g/cm3(Predicted)
• Storage Temp.: -20?C Freezer
• PKA: 12.71±0.70(Predicted)
• CAS DataBase Reference: Methyla-D-laminarabioside(CAS DataBase Reference)
• NIST Chemistry Reference: Methyla-D-laminarabioside(7115-19-7)
• EPA Substance Registry System: Methyla-D-laminarabioside(7115-19-7)

Safety Data

• Hazardous Substances Data: 7115-19-7(Hazardous Substances Data)

Usage

Chemical Properties

WHite Solid

Uses

Methyl α-D-laminaribioside (cas# 7115-19-7) is a compound useful in organic synthesis.

Upstream product

• 14218-11-2 2,3,4,6-tetra-O-benzoylglucosyl bromide 
• 20750-02-1 methyl 2-O-acetyl-4,6-O-benzylidene-β,D-glucopyranoside 
• 67-56-1 methanol 
• 195715-87-8 Acetic acid (2R,3R,4S,5R,6S)-5-acetoxy-2-acetoxymethyl-6-fluoro-4-((2S,3R,4S,5R,6R)-3,4,5-triacetoxy-6-acetoxymethyl-tetrahydro-pyran-2-yloxy)-tetrahydro-pyran-3-yl ester 
• 29842-30-6 laminarihexaose 
• 3256-04-0 laminaritriose 
• 26212-72-6 laminaritetraose 
• 23743-55-7 laminaripentaose 
• 709-50-2 methyl beta-D-glucopyranoside 
• 59-56-3 α-D-glucopyranosyl-1-phosphate 
• 25577-40-6 methyl 2-O-acetyl-4,6-O-benzylidene-α,D-glucopyranoside 
• 3162-96-7 methyl 4,6-O-benzylidene-α-D-glucopyranoside 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 
• 3396-99-4 methyl α-D-galactopyranoside 

Downstream Products

• 7322-42-1 methyl O-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)-(1->3)-2,4,6-tri-O-acetyl-α-D-galactopyranoside 
• 78797-79-2 methyl 2,4-di-O-acetyl-6-O-p-tolylsulfonyl-3-O-(2,3,4-tri-O-acetyl-6-O-p-tolylsulfonyl-β-D-glucopyranosyl)-β-D-glucopyranoside 
• 78797-77-0 methyl 2,4-di-O-acetyl-3-O-(2,3,4-tri-O-acetyl-6-O-trityl-β-D-glucopyranosyl)-6-O-trityl-β-D-glucopyranoside 

Relevant articles and documents

Regio- and stereochemical controlled koenigs-knorr-type monoglycosylation of secondary hydroxy groups in carbohydrates utilizing the high site recognition ability of organotin catalysts

The catalytic regio- and stereoselective monoglycosylation of carbohydrates using organotin catalysts is demonstrated. The one-step reaction affords various oligosaccharides linked at the secondary hydroxy group in high chemical yield and good regio- and stereoselectivities. The regioselectivity of the glycosylation is shown to depend on the spatial arrangement of the hydroxy groups in the carbohydrates. Copyright

An exo-β-(1→3)-d-galactanase from Streptomyces sp. provides insights into type II arabinogalactan structure

An exo-β-(1→3)-d-galactanase (SGalase1) that specifically cleaves the β-(1→3)-d-galactan backbone of arabinogalactan-proteins (AGPs) was isolated from culture filtrates of a soil Streptomyces sp. Internal peptide sequence information was used to clone and recombinantly express the gene in E. coli. The molecular mass of the isolated enzyme was ～45 kDa, similar to the 48.2 kDa mass predicted from the amino acid sequence. The pI, pH and temperature optima for the enzyme were ～7.45, 3.8 and 48 °C, respectively. The native and recombinant enzymes specifically hydrolysed β-(1→3)-d- galacto-oligo- or poly-saccharides from the upstream (non-reducing) end, typical of an exo-acting enzyme. A second homologous Streptomyces gene (SGalase2) was also cloned and expressed. SGalase2 was similar in size (47.9 kDa) and enzyme activity to SGalase1 but differed in its pH optimum (pH 5). Both SGalase1 and SGalase2 are predicted to belong to the CAZy glycosyl hydrolase family GH 43 based on activity, sequence homology and phylogenetic analysis. The K m and Vmax of the native exo-β-(1→3)-d- galactanase for de-arabinosylated gum arabic (dGA) were 19 mg/ml and 9.7 μmol d-Gal/min/mg protein, respectively. The activity of these enzymes is well suited for the study of type II galactan structures and provides an important tool for the investigation of the biological role of AGPs in plants. De-arabinosylated gum arabic (dGA) was used as a model to investigate the use of these enzymes in defining type II galactan structure. Exhaustive hydrolysis of dGA resulted in a limited number of oligosaccharide products with a trisaccharide of Gal2GlcA1 predominating.

Thermus thermophilus glycosynthases for the efficient synthesis of galactosyl and glucosyl β-(1→3)-glycosides

Inverting mutant glycosynthases were designed according to the Withers strategy, starting from wild-type Thermus thermophilus retaining Tt-β-Gly glycosidase. Directed mutagenesis of catalytic nucleophile glutamate 338 by alanine, serine, and glycine afforded the E338A, E338S, and E338G mutant enzymes, respectively. As was to be expected, the mutants were unable to catalyze the hydrolysis of the transglycosidation products. In agreement with previous results, the E338S and E338G catalysts were much more efficient than E338A. Moreover, our results showed that these enzymes were inactive in the hydrolysis of the α-D-glycopyranosyl fluorides used as donors, and so suitable experimental conditions, under which the rate of spontaneous hydrolysis of the donor was considerably lower than that of enzymatic transglycosidation, provided galactosyl and glucosyl β-(1→3)-glycosides in yields of up to 90%. The structure of native Tt-β-Gly available in the Protein Data Bank offers a good basis for interpretation of our results by means of molecular modeling. Thus, in the case of the E338S mutant, a lower energy of the system was obtained when the donor and the acceptor were in the right position to form the β-(1→3)-glycosidic bond. Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005.