110891-71-9

Upstream product

• 105600-45-1 p-nitrophenyl 2,4,6-tri-O-acetyl-3-O-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-α-D-mannopyranoside 
• 93979-05-6 p-nitrophenyl 2-O-benzoyl-4,6-O-benzylidene-3-O-(2,3,4,6-tetra-O-benzoyl-α-D-mannopyranosyl)-α-D-mannopyranoside 
• 14218-11-2 2,3,4,6-Tetra-O-benzoyl-α-D-mannopyranosyl bromide 
• 105600-43-9 4-nitrophenyl 4,6-di-O-acetyl-α-D-mannopyranoside 
• 80264-82-0 p-nitrophenyl 2,3-O-isopropylidene-α-D-mannopyranoside 
• 186665-12-3 ethyl O-β-D-galactopyranosyl-(1-4)-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-1-thio-β-D-glucopyranoside 
• 7493-95-0 4-nitrophenyl α-D-galactoside 
• 210281-95-1 β-D-mannopyranosyl fluoride 
• 10357-27-4 4-nitrophenyl-α-D-mannopyranoside 
• 439-03-2 2,3,4,6-tetra-O-acetyl-β-D-mannopyranosyl fluoride 
• 105600-44-0 p-nitrophenyl 2,4,6-tri-O-acetyl-α-D-mannopyranoside 
• 105600-42-8 p-nitrophenyl 4,6-di-O-acetyl-2,3-O-isopropylidene-α-D-mannopyranoside 
• 58056-41-0 p-nitrophenyl 4,6-O-benzylidene-α-D-mannopyranoside 
• 81562-01-8 p-nitrophenyl 2-O-benzoyl-4,6-O-benzylidene-α-D-mannopyranoside 

Downstream Products

• 1402245-97-9 C₄₄H₅₅NO₂₈ 
• 1402245-98-0 C₄₄H₅₅NO₂₈ 
• 1402245-87-7 C₂₄H₃₅NO₁₈ 
• 1402245-86-6 C₂₄H₃₅NO₁₈ 
• 188302-04-7 p-aminophenyl 3-O-(α-D-galactopyranosyl)-α-D-galactopyranoside 

Relevant academic research and scientific papers

Glycosidase-catalysed synthesis of di- and trisaccharide derivatives related to antigens involved in the hyperacute rejection of xenotransplants

A convenient enzymatic procedure, suitable for large scale preparation of the β-thioethyl 2-N-Teoc-derivative of Galα1-3Galβ1-4GlcNAc, is described (Teoc = 2,2,2-trichloroethoxycarbonyl). β-D-Galactosidase from Bullera singularis was used for the specific

Transglycosylation activity of α-D-galactosidase from Trichoderma reesei. An investigation of the active site

The transglycosylation reaction catalyzed by α-D-galactosidase from the mycelial fungus Trichoderma reesei was studied using p-nitrophenyl α-D- galactopyranoside (PNPG). An aliphatic alcohol or the substrate itself can be an acceptor of the galactose residue in this reaction. The transglycosylation products were identified as alkyl galactosides in the case of alcohols or as galactobioside and galactotrioside in the case of PNPG. The transglycosylation rates follow a first-order equation with respect to the alcohol concentrations except for methanol. Affinities of some substrates were estimated from their K(i) values in the reaction of the enzyme with PNPG. Transglycosylation of the substrate suggests a model for the enzyme active center. It is proposed that the active center includes two galactose- binding sites and a hydrophobic site.

α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima

Broad regioselectivity of α-galactosidase from Thermotoga maritima (TmGal36A) is a limiting factor for application of the enzyme in the directed synthesis of oligogalactosides. However, this property can be used as a convenient tool in studies of thermodynamics of a glycosidic bond. Here, a novel approach to energy difference estimation is suggested. Both transglycosylation and hydrolysis of three types of galactosidic linkages were investigated using total kinetics of formation and hydrolysis of pNP-galactobiosides catalysed by monomeric glycoside hydrolase family 36 α-galactosidase from T. maritima, a retaining exo-acting glycoside hydrolase. We have estimated transition state free energy differences between the 1,2- and 1,3-linkage (ΔΔG?0 values were equal 5.34 ± 0.85 kJ/mol) and between 1,6-linkage and 1,3-linkage (ΔΔG?0 = 1.46 ± 0.23 kJ/mol) in pNP-galactobiosides over the course of the reaction catalysed by TmGal36A. Using the free energy difference for formation and hydrolysis of glycosidic linkages (ΔΔG?F - ΔΔG?H), we found that the 1,2-linkage was 2.93 ± 0.47 kJ/mol higher in free energy than the 1,3-linkage, and the 1,6-linkage 4.44 ± 0.71 kJ/mol lower.

α-Galactobiosyl units: Thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 α-galactosidase from Thermotoga maritima

Broad regioselectivity of α-galactosidase from Thermotoga maritima (TmGal36A) is a limiting factor for application of the enzyme in the directed synthesis of oligogalactosides. However, this property can be used as a convenient tool in studies of thermodynamics of a glycosidic bond. Here, a novel approach to energy difference estimation is suggested. Both transglycosylation and hydrolysis of three types of galactosidic linkages were investigated using total kinetics of formation and hydrolysis of pNP-galactobiosides catalysed by monomeric glycoside hydrolase family 36 α-galactosidase from T. maritima, a retaining exo-acting glycoside hydrolase. We have estimated transition state free energy differences between the 1,2- and 1,3-linkage (ΔΔG?0 values were equal 5.34 ± 0.85 kJ/mol) and between 1,6-linkage and 1,3-linkage (ΔΔG?0 = 1.46 ± 0.23 kJ/mol) in pNP-galactobiosides over the course of the reaction catalysed by TmGal36A. Using the free energy difference for formation and hydrolysis of glycosidic linkages (ΔΔG?F - ΔΔG?H), we found that the 1,2-linkage was 2.93 ± 0.47 kJ/mol higher in free energy than the 1,3-linkage, and the 1,6-linkage 4.44 ± 0.71 kJ/mol lower.

Creation of an α-mannosynthase from a broad glycosidase scaffold

α-Mannosides made easy: Mutation of a family-GH31 α-glucosidase that displays plasticity to alterations at the 2-OH position of donor substrates created an efficient α-mannoside-synthesizing biocatalyst. A simple fluoride donor reagent was used for the synthesis of a range of mono-α-mannosylated conjugates using the α-mannosynthase displaying low (unwanted) oligomerization activity. Copyright

α-Galactosyl fluoride in transfer reactions mediated by the green coffee beans α-galactosidase in ice

We show that the yields in saccharide synthesis by tranglycosylation with α-galactosidase from green coffee beans can be greatly enhanced when working in ice. Thus, methyl α-D-galactopyranosyl-(1 → 3)-α-D-galactopyranoside (3a) produced by reaction of α-D-galactopyranosyl fluoride 1 with methyl α-D-galactopyranoside (2) is obtained with 51% yield in ice while only 29% is synthesized at 37°C. This result, already previously found by others with proteases and by us with a β-galactosidase appears to be a general property of hydrolases.

Comparative study of new α-galactosidases in transglycosylation reactions

We have studied the potential of several newly cloned α-galactosidases to catalyze the regioselective synthesis of disaccharides using 4-nitrophenylgalactoside as a donor. The kinetics of the reactions were followed by in situ NMR spectroscopy. The following thermophilic enzymes have been tested: Aga A and an isoenzyme Aga B obtained from the strain KVE39 and Aga 285 from the strain IT285 of Bacillus stearothermophilus; Aga T is an α-galactosidase from Thermus brockianus (strain IT360). Two other non-thermophilic α-galactosidases have also been evaluated: Aga 1 (Streptococcus mutans, strain Ingbritt) and Raf A (Escherichia coli, strain D1021). For all of the enzymes studied, high regioselectivity was observed leading to two (1 → 6)-disaccharides: 4-nitrophenyl α-D-galactopyranosyl-(1 → 6)-α-D-galactopyranoside and methyl α-D-galactopyranosyl-(1 → 6)-α-D-galactopyranoside, which were obtained in 54% (Aga B) and 20% (Aga T) yields, respectively. (C) 2000 Elsevier Science Ltd.

Chemical and enzymatic synthesis of glycoconjugates 5: One-pot regioselective synthesis of bioactive galactobiosides using a clonezyme(TM) thermophilic glycosidase library

Enzymatic synthesis of galactobiosides using a versatile CLONEZYME(TM) thermostable glycosidase library was studied. One-pot transglycosylation reactions were demonstrated to synthesize β(1→4), β(1→6), and α(1→6) disaccharide sequences with high regiosele

Chemoenzymatic synthesis of Galα1-3Gal, Galα1-3Galβ1-4GlcNAc, and their PEG-conjugates

Galα1-3Gal-pNP was prepared enzymatically from Gal-pNP using α-galactosidase from coffee beans. PEG was attached after the reduction of nitro group into amino group to give Galα1-3Gal-PEG conjugate. After removing the pNP group in Galα1-3Gal-pNP, the obtained disaccharide was used for the synthesis of Galα1-3Galβ1-4GlcNAc and corresponding trisaccharide-PEG conjugate.