6659-40-1

Usage

Uses

Used in Pharmaceutical Industry:
Uridine diphosphate 2-deoxyglucose is used as a therapeutic agent for its potential role in modulating cellular metabolism and energy production. Its involvement in glycosylation processes makes it a promising candidate for the development of drugs targeting various diseases, including metabolic disorders and certain types of cancer.
Used in Biotechnology Industry:
In the biotechnology sector, UDP-Glc is utilized as a key component in the biosynthesis of polysaccharides, which are essential for the structural integrity and function of bacterial, fungal, and plant cell walls. Its role in these processes makes it a valuable tool for the production of biomaterials and the development of novel bioprocesses.
Used in Research and Development:
Uridine diphosphate 2-deoxyglucose is employed as a research tool in the study of glycosylation and its impact on protein and lipid function. It is also used to investigate the regulation of cellular metabolism, energy production, and immune response, contributing to a deeper understanding of these biological processes and their implications in health and disease.
Used in Diagnostic Applications:
UDP-Glc can be used as a diagnostic marker to assess the status of cellular metabolism and energy production, as well as the integrity of the immune response. Its measurement in biological samples can provide valuable insights into the health of an individual and the presence of certain diseases or conditions.

InChI:InChI=1/C15H24N2O16P2/c18-4-7-11(21)12(22)13(23)14(31-7)32-35(27,28)33-34(25,26)29-5-8-6(19)3-10(30-8)17-2-1-9(20)16-15(17)24/h1-2,6-8,10-14,18-19,21-23H,3-5H2,(H,25,26)(H,27,28)(H,16,20,24)/t6-,7+,8+,10+,11+,12-,13+,14+/m0/s1

Upstream product

• 42155-08-8 2’-deoxyuridine 5’-monophosphate disodium salt 
• 57-50-1 Sucrose 
• 1173-82-6 2'-deoxyuridine-5'-triphosphate 
• 59-56-3 α-D-glucopyranosyl-1-phosphate 

Relevant academic research and scientific papers

Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from: Streptococcus pneumonia serotype 23F

Glucose-1-phosphate thymidylyltransferase (Cps23FL) from Streptococcus pneumonia serotype 23F is the initial enzyme that catalyses the thymidylyl transfer reaction in prokaryotic deoxythymidine diphosphate-l-rhamnose (dTDP-Rha) biosynthetic pathway. In this study, the broad substrate specificity of Cps23FL towards six glucose-1-phosphates and nine nucleoside triphosphates as substrates was systematically explored, eventually providing access to nineteen sugar nucleotide analogs.

A chemoenzymatic route to synthesize unnatural sugar nucleotides using a novel N-acetylglucosamine-1-phosphate pyrophosphorylase from Camphylobacter jejuni NCTC 11168

A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized.

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.

Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12

N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report th

Combined enzymatic synthesis of nucleotide (deoxy) sugars from sucrose and nucleoside monophosphates

The synthesis of NDP-glucose 3a-d (N = A, C, U, dU) with sucrose synthase B was combined with the enzymatic synthesis of nucleoside diphosphates 2a-d from their corresponding nucleoside monophosphates 1a-d by different kinases A. Further combination with