16375-63-6

Upstream product

• 153448-93-2 2,3,4-tri-O-acetyl-6-deoxy-α-D-galactopyranosyl 1-phosphate dibenzyl ester 
• 73-34-7 D-Fucose 
• 63-39-8 UTP 
• 1476-50-2 uridine 5'-triphosphate trisodium salt 
• 157365-62-3 2,3,4-tri-O-acetyl-6-deoxy-α-D-galactopyranose 
• 81276-27-9 Gal6deoxy-1-P 
• 28915-80-2 2,3,4-tri-O-acetyl-6-deoxy-D-galactopyranose 
• 51921-33-6 1,2,3,4-tetra-O-acetyl-D-fucopyranose 
• 5158-64-5 2,3,4-tri-O-acetyl-D-fucopyranosyl bromide 

Relevant academic research and scientific papers

Biosynthesis of nucleotide sugars by a promiscuous UDP-sugar pyrophosphorylase from Arabidopsis thaliana (AtUSP)

Nucleotide sugars are activated forms of monosaccharides and key intermediates of carbohydrate metabolism in all organisms. The availability of structurally diverse nucleotide sugars is particularly important for the characterization of glycosyltransferases. Given that limited methods are available for preparation of nucleotide sugars, especially their useful non-natural derivatives, we introduced herein an efficient one-step three-enzyme catalytic system for the synthesis of nucleotide sugars from monosaccharides. In this study, a promiscuous UDP-sugar pyrophosphorylase (USP) from Arabidopsis thaliana (AtUSP) was used with a galactokinase from Streptococcus pneumoniae TIGR4 (SpGalK) and an inorganic pyrophosphatase (PPase) to effectively synthesize four UDP-sugars. AtUSP has better tolerance for C4-derivatives of Gal-1-P compared to UDP-glucose pyrophosphorylase from S. pneumoniae TIGR4 (SpGalU). Besides, the nucleotide substrate specificity and kinetic parameters of AtUSP were systematically studied. AtUSP exhibited considerable activity toward UTP, dUTP and dTTP, the yield of which was 87%, 85% and 84%, respectively. These results provide abundant information for better understanding of the relationship between substrate specificity and structural features of AtUSP.

One-pot three-enzyme synthesis of UDP-Glc, UDP-Gal, and their derivatives

A UTP-glucose-1-phosphate uridylyltransferase (SpGalU) and a galactokinase (SpGalK) were cloned from Streptococcus pneumoniae TIGR4 and were successfully used to synthesize UDP-galactose (UDP-Gal), UDP-glucose (UDP-Glc), and their derivatives in an efficient one-pot reaction system. The reaction conditions for the one-pot multi-enzyme synthesis were optimized and nine UDP-Glc/Gal derivatives were synthesized. Using this system, six unnatural UDP-Gal derivatives, including UDP-2-deoxy-Galactose and UDP-GalN3 which were not accepted by other approach, can be synthesized efficiently in a one pot fashion. More interestingly, this is the first time it has been reported that UDP-Glc can be synthesized in a simpler one-pot three-enzyme synthesis reaction system.

Rapid conversion of unprotected galactose analogs to their UDP-derivatives for use in the chemoenzymatic synthesis of unnatural oligosaccharides

The rapid conversion of D-galactose, its 2-deoxy, 3-deoxy, 4-deoxy and 6-deoxy derivatives and L-arabinose to their UDP-derivatives (2-7) is described. The procedure involves the in situ preparation of the per-O-trimethylsilylated glycopyranosyl iodides and their direct reaction with UDP. All six sugar nucleotides were active as substrates for β(1→4)-galactosyltransferase and were used to enzymatically prepare N-acetyllactosamine (8) and five of its analogs (9-13).

Enzymic transfer of 6-modified D-galactosyl residues: Synthesis of biantennary penta- and hepta-saccharides having two 6-deoxy-D-galactose residues at the nonreducing end and evaluation of 6-deoxy-D-galactosyl transfer to glycoprotein using bovine β-(1 4)-galactosyltransferase and UDP-6-deoxy-D-galactose

UDP-6-Deoxy-D-galactose and UDP-6-deoxy-6-fluoro-D-galactose were synthesized and their transfer to 2-acetamido-2-deoxy-D-glucose (N-acetyl-D-glucosamine) by β-(1 → 4)-galactosyltransferase was examined. The transfer rates of 6-deoxy-D-galactose and 6-deoxy-6-fluoro-D-galactose were 1.3 and 0.2% of that of D-galactosyl transfer, respectively. The 2-acetamido-4-O-(6-deoxy-β-D-galactopyranosyl)-2-deoxy-D-glucopyranos e (6'-deoxy-N-acetyllactosamine) and methyl 2-acetamido-4-O-(6-deoxy-6-fluoro-β-D-galactopyranosyl)-2-deoxy-D-glu copyranoside (6'-deoxy-6'-fluoro-N-acetyllactosamine) were synthesized enzymatically in 30 and 59% yields, respectively. Further, 6-deoxy-D-galactose could be completely transferred to N-linked type biantennary oligosaccharides having two N-acetyl-D-glucosaminyl residues at the nonreducing end to give the corresponding penta- and hepta-saccharides in 55 and 57% yields, respectively. An assay of 6-deoxy-D-galactosyl transfer using asialo agalacto α1-acid glycoprotein as an acceptor suggested that 6-deoxy-D-galactose was transferred to about 30% of the N-acetyl-D-glucosaminyl residues in the N-linked oligosaccharides of the glycoprotein.

Synthesis of uridine 5′(α-D-fucopyranosyl diphosphate) and (digitoxigenin-3β-yl)-β-D-fucopyranoside and enzymatic β-D-fucosylation of cardenolide aglycones in Digitalis lanata

The phosphorylation of 2,3,4-tri-Oacetyl-α-D-fucopyranose with o-phenylene phosphochloridate yielded α-D-fucopyranosyl phosphate which was used for condensation with undine 5′-monophosphomorpholidate to give uridine 5′-(α-D-fucopyranosyl diphosphate) (UDP-α-D-fucose). A crude enzyme preparation from young leaves of Digitalis lanata EHRH has been shown to catalyze the transfer of D-fucose from synthetic UDP-α-D-fucose to cardenolide aglycones, such as digitoxigenin. The reaction product was identified and characterized by chemical synthesis, HPLC, and spectral methods as the 3 β-O-β-D-fucopyranoside of digitoxigenin (digiproside). Copyright