2152-75-2

Usage

Uses

Used in Enzymatic Synthesis:
ALPHA-D-GLUCOSAMINE 1-PHOSPHATE is used as a substrate for the enzymatic α-glucosaminylation of maltooligosaccharides. This process is catalyzed by phosphorylase, an enzyme that facilitates the transfer of glucosamine residues to form complex carbohydrate structures.
Used in Pharmaceutical Industry:
ALPHA-D-GLUCOSAMINE 1-PHOSPHATE is utilized in the development of drugs targeting various medical conditions. Its role in the synthesis of glycosaminoglycans makes it a potential candidate for therapeutic applications in treating diseases associated with the dysregulation of these molecules, such as arthritis, cancer, and certain genetic disorders.
Used in Research and Development:
This phosphorylated glucosamine is also employed in research settings to study the mechanisms of glycosaminoglycan synthesis and its implications in cellular processes. Understanding the role of ALPHA-D-GLUCOSAMINE 1-PHOSPHATE in these pathways can lead to the discovery of novel therapeutic strategies and the development of new drugs for various diseases.

InChI:InChI=1/C6H14NO8P/c7-3-5(10)4(9)2(1-8)14-6(3)15-16(11,12)13/h2-6,8-10H,1,7H2,(H2,11,12,13)/t2-,3-,4-,5-,6-/m1/s1

Upstream product

• 6665-06-1 D-glucosamine-6-phosphate 
• 35946-68-0 O³,O⁴,O⁶-triacetyl-2-amino-O¹-diphenoxyphosphoryl-2-deoxy-α-D-glucopyranose; hydrochloride 
• 79184-08-0 3,4,6-tri-O-acetyl-2-acetamido-1-O-[bis(benzyloxy)phophoryl]-2-deoxy-α-D-glucopyranose 
• 884856-12-6 (2-azido-3,4,6-tri-O-benzyl-2-deoxy-α-D-glucpyranosyl) dibenzyl phosphate 
• 66-84-2 D-(+)-glucosamine hydrochloride 
• 1078691-95-8 (+)-D-glucosamine hydrochloride 
• 171032-74-9 1,3,4,6-tetra-O-acetyl-2-azido-2-deoxy-D-glucopyranose 
• 1355005-35-4 2-azido-2-deoxy-D-glucopyranose-3,4,6-triacetate-1-(dihydrogen phosphate) 
• 1334525-86-8 2-azido-2-deoxy-D-glucopyranose-1-(dihydrogen phosphate) 
• 90-76-6 D-galactosamine 
• 79781-69-4 2-azido-3,4,6-tri-O-benzyl-2-deoxy-D-galactopyranose 

Downstream Products

• 1109-79-1 uridine 5'-(2-amino-2-deoxy-α-D-glucopyranosyl)-diphosphate 
• 28446-21-1 N-acetylglucosamine-1-phosphate 
• 528-04-1 uridine 5'-diphospho-N-acetylglucosamine 
• 16503-17-6 [13C]-N-acetylglucosamine-1-phosphate 
• 17479-06-0 uridine 5'-(2-amino-2-deoxy-α-D-galactopyranosyl diphosphate) 
• 92283-18-6 3,4,6-tri-O-acetyl-2-acetamido-2-deoxy-α-D-galactopyranosyl dihydrogen phosphate 
• 528-04-1 uridine-5'-diphospho-N-acetyl-D-galactosamine 

Relevant academic research and scientific papers

Allosteric Modulation of the Faecalibacterium prausnitzii Hepatitis Delta Virus-like Ribozyme by Glucosamine 6-Phosphate: The Substrate of the Adjacent Gene Product

Self-cleaving ribozymes were discovered 30 years ago and have been found throughout nature, from bacteria to animals, but little is known about their biological functions and regulation, particularly how cofactors and metabolites alter their activity. A hepatitis delta virus-like self-cleaving ribozyme maps upstream of a phosphoglucosamine mutase (glmM) open reading frame in the genome of the human gut bacterium Faecalibacterium prausnitzii. The presence of a ribozyme in the untranslated region of glmM suggests a regulation mechanism of gene expression. In the bacterial hexosamine biosynthesis pathway, the enzyme glmM catalyzes the isomerization of glucosamine 6-phosphate into glucosamine 1-phosphate. In this study, we investigated the effect of these metabolites on the co-transcriptional self-cleavage rate of the ribozyme. Our results suggest that glucosamine 6-phosphate, but not glucosamine 1-phosphate, is an allosteric ligand that increases the self-cleavage rate of drz-Fpra-1, providing the first known example of allosteric modulation of a self-cleaving ribozyme by the substrate of the adjacent gene product. Given that the ribozyme is activated by the glmM substrate, but not the product, this allosteric modulation may represent a potential feed-forward mechanism of gene expression regulation in bacteria.

A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase

Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans. Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of t

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.

Artificial N-functionalized UDP-glucosamine analogues as modified substrates for N-acetylglucosaminyl transferases

Analogues of UDP-GlcNAc modified at the 2-acetamido group of the GlcNAc moiety were prepared in order to study their role in the mechanism of N-acetylglucosaminyl transferase mediated glycosylation reactions. The structural analogues with N-formyl-, N-pro

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.

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.

CHEMICAL SYNTHESIS OF PHOSPHORYLATED FUNDAMENTAL STRUCTURE OF LIPID A

1-α-Monophosphate (2), 4'-monophosphate (3), and 1-α,4'-diphosphate (4) of 6-O-(2-deoxy-2-tetradecanoylamino-6-O-tetradecanoyl-β-D-glucopyranosyl)-2-deoxy-2-tetradecanoylamino-3,4-di-O-tetradecanoyl-D-glucopyranose were prepared in order to elucidate the