22916-34-3

Upstream product

• 90-76-6 D-galactosamine 
• 79781-69-4 2-azido-3,4,6-tri-O-benzyl-2-deoxy-D-galactopyranose 

Downstream Products

• 16503-17-6 [13C]-N-acetylglucosamine-1-phosphate 
• 17479-06-0 uridine 5'-(2-amino-2-deoxy-α-D-galactopyranosyl diphosphate) 
• 528-04-1 uridine-5'-diphospho-N-acetyl-D-galactosamine 
• 92283-18-6 3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate 

Relevant academic research and scientific papers

Studies on the substrate specificity of Escherichia coli galactokinase

(Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.

Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms

Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a d-galactosyl-β1-3-N-acetyl-d-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2-3-sialyltransferase or an α2-6-sialyltransferase.

A highly efficient galactokinase from Bifidobacterium infantis with broad substrate specificity

Galactokinase (GalK), particularly GalK from Escherichia coli, has been widely employed for the synthesis of sugar-1-phosphates. In this study, a GalK from Bifidobacterium infantis ATCC 15697 (BiGalK) was cloned and over-expressed with a yield of over 80 mg/L cell cultures. The kcat/Km value of recombinant BiGalK toward galactose (164 s-1 mM -1) is 296 times higher than that of GalK from E. coli, indicating that BiGalK is much more efficient in the phosphorylation of galactose. The enzyme also exhibits activity toward galacturonic acid, which has never been observed on other wild type GalKs. Further activity assays showed that BiGalK has broad substrate specificity toward both sugars and phosphate donors. These features make BiGalK an attractive candidate for the large scale preparation of galactose-1-phosphate and derivatives.

Syntheses of unnatural N-substituted UDP-galactosamines as alternative substrates for N-acetylgalactosaminyl transferases

UDP-GalNAc analogues with slight modifications in the 2-acetamido group of the GalNAc moiety are prepared in order to study their role in the mechanism of the N-acetylgalactosaminyl transferase mediated glycosylation step. The analogues with N-propionyl-,

One-step, stereocontrolled synthesis of glycosyl 1-phosphates, uridine- 5'-diphosphogalactose, and uridine-5'-diphosphoglucose from unprotected glycosyl donors

The reaction of 2-(1,2-trans-glycopyranosyloxy)-3-methoxypyridines (MOP glycosides) with phosphoric acid leads to the corresponding 1,2-cis-1- phosphates in good yield and excellent stereoselectivity. 1-Phosphate esters of α-D-glucopyranose, α-D-galactopyranose, and 2-azido-2-deoxy-α-D- galactopyranose were thus prepared without recourse to protective groups. In the L-fucose series, the major product was the α-L-fucosyl 1-phosphate. An alternative method that relies on neighboring group participation allowed the preparation of a protected β-L-fucosyl 1-phosphate. Reaction of unprotected β-D-glucopyranosyloxy and β-D-galactopyranosyloxy MOP donors with uridine diphosphoric acid gave UDP-Glc and UDP-Gal with preponderance of the desired α-anomeric configuration.