28508-02-3

Basic information

• Product Name: URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)]
• Synonyms: URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)]
• CAS NO: 28508-02-3
• Molecular Formula: C17H27N3O17P2
• Molecular Weight: 617.44
• Mol File: 28508-02-3.mol

Chemical Properties

• Appearance: /
• Density: 1.86g/cm³
• Refractive Index: 1.651
• CAS DataBase Reference: URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)](CAS DataBase Reference)
• NIST Chemistry Reference: URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)](28508-02-3)
• EPA Substance Registry System: URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)](28508-02-3)

Safety Data

• Hazardous Substances Data: 28508-02-3(Hazardous Substances Data)

Usage

Uses

Used in Metabolic Research:
Uridine diphosphate N-acetyl-D-glucosamine, [glucosamine-14C(U)] is used as a research tool for studying the biosynthesis and degradation of complex carbohydrates. The radioactive isotope 14C allows for the tracing and quantifying of glucosamine incorporation into biological molecules, providing valuable insights into the role of URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)] in cellular processes.
Used in Pharmaceutical Development:
In the pharmaceutical industry, Uridine diphosphate N-acetyl-D-glucosamine, [glucosamine-14C(U)] is used as a key component in the development of therapeutic agents targeting conditions such as osteoarthritis and inflammatory disorders. Its role in glycosylation processes and its incorporation into biological molecules make it a promising candidate for the creation of novel treatments.
Used in Diagnostic Applications:
Uridine diphosphate N-acetyl-D-glucosamine, [glucosamine-14C(U)] can be employed as a diagnostic agent to assess the activity of enzymes involved in glycosylation processes. By monitoring the incorporation of the radioactive isotope 14C into biological molecules, researchers can gain insights into the functioning of these enzymes and identify potential abnormalities or deficiencies.
Used in Biochemical Education:
In the field of biochemical education, Uridine diphosphate N-acetyl-D-glucosamine, [glucosamine-14C(U)] serves as an essential teaching tool to illustrate the principles of glycosylation and the synthesis of complex carbohydrates. The radioactive isotope 14C provides a unique opportunity for students to visualize and understand the incorporation of glucosamine into biological molecules, enhancing their comprehension of these processes.

InChI:InChI=1/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16+/m1/s1

Upstream product

• 1363386-22-4 uridine 5'-diphospho-2-azido-2-deoxy-α-D-mannopyranoside 
• 1366133-51-8 UDP-ManN 
• 75-36-5 acetyl chloride 
• 97604-58-5 2-azido-2-deoxy-D-mannopyranose 
• 63-39-8 UTP 
• 28446-21-1 N-acetylglucosamine-1-phosphate 
• 72-87-7 N-acetyl-D-galactosamine 
• 1476-50-2 uridine 5'-triphosphate trisodium salt 
• 528-04-1 uridine 5'-diphospho-N-acetylglucosamine 
• 1211328-11-8 UDP-GalfNAc 
• 58-97-9 5'-Uridylic Acid 
• 2152-75-2 2-amino-2-deoxy-α-D-galactopyranosyl 1-phosphate 
• 27908-36-7 uridine 5'-monophosphate morpholidate 
• 219564-76-8 Acetic acid (3aR,5R,6R,7R,7aR)-6-acetoxy-5-acetoxymethyl-2-trifluoromethyl-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d]oxazol-7-yl ester 

Downstream Products

• 528-04-1 uridine 5'-diphospho-2-acetamido-2-deoxy-α-D-mannopyranoside 
• 1398147-44-8 C₃₃H₄₈NO₂₃^(1-)*Na⁽¹⁺⁾ 
• 1448012-76-7 GlcA-β-1,4-GlcNAc-α-1,4-GlcA-pNP 
• 16124-22-4 UDP-N-acetylmuramyl-L-alanyl-γ-D-glutamyl-m-diaminopimelyl-D-alanyl-D-alanine 
• 87866-15-7 Gal-β1,3[GlcNAc-β1,6]-GalNAc-α1-OBn 

Relevant articles and documents

Gram-scale production of sugar nucleotides and their derivatives

Here, we report a practical sugar nucleotide production strategy that combined a high-concentrated multi-enzyme catalyzed reaction and a robust chromatography-free selective precipitation purification process. Twelve sugar nucleotides were synthesized on a gram scale with a purity up to 98%.

Enzymatic Synthesis of Human Milk Fucosides α1,2-Fucosyl para-Lacto-N-Hexaose and its Isomeric Derivatives

Enzymatic synthesis of para-lacto-N-hexaose and its isomeric structures as well as those α1,2-fucosylated variants naturally occurring in human milk oligosaccharide (HMOs) was achieved using a sequential one-pot enzymatic system. Three glycosylation routes comprising bacterial glycosyltransferases and corresponding sugar-nucleotide-generating enzymes were developed to facilitate efficient production of extended type-1 and type-2 N-acetyllactosamine (LacNAc) backbones and hybrid chains. Further fucosylation efficiency of two α1,2-fucosyltransferases on both type-1 and type-2 chains of the hexasaccharide was investigated to achieve practical synthesis of the fucosylated glycans. The availability of structurally defined HMOs offers a practical approach for investigating future biological applications. (Figure presented.).

Characterization and mutational analysis of two UDP-galactose 4-epimerases in Streptococcus pneumoniae TIGR4

Current clinical treatments for pneumococcal infections have many limitations and are faced with many challenges. New capsular polysaccharide structures must be explored to cope with diseases caused by different serotypes of Streptococcus pneumoniae. UDP-galactose 4-epimerase (GalE) is an essential enzyme involved in polysaccharide synthesis. It is an important virulence factor in many bacterial pathogens. In this study, we found that two genes (galEsp1 and galEsp2) are responsible for galactose metabolism in pathogenic S. pneumoniae TIGR4. Both GalESp1 and GalESp2 were shown to catalyze the epimerization of UDP-glucose (UDP-Glc)/UDP-galactose (UDP-Gal), but only GalESp2 was shown to catalyze the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc)/UDP-N-acetylgalactosamine (UDP-GalNAc). Interestingly, GalESp2 had 3-fold higher epimerase activity toward UDP-Glc/UDP-Gal than GalESp1. The biochemical properties of GalESp2 were studied. GalESp2 was stable over a wide range of temperatures, between 30 and 70°C, at pH 8.0. The K86G substitution caused GalESp2 to lose its epimerase activity toward UDP-Glc and UDP-Gal; however, substitution C300Y in GalESp2 resulted in only decreased activity toward UDP-GlcNAc and UDP-GalNAc. These results indicate that the Lys86 residue plays a critical role in the activity and substrate specificity of GalESp2.

Efficient chemoenzymatic synthesis of uridine 5′-diphosphate N-acetylglucosamine and uridine 5′-diphosphate N-trifluoacetyl glucosamine with three recombinant enzymes

Uridine 5′-diphosphate N-acetylglucosamine (UDP-GlcNAc) is a natural UDP-monosaccharide donor for bacterial glycosyltransferases, while uridine 5′-diphosphate N-trifluoacetyl glucosamine (UDP-GlcNTFA) is its synthetic mimic. The chemoenzymatic synthesis of UDP-GlcNAc and UDP-GlcNTFA was attempted by three recombinant enzymes. Recombinant N-acetylhexosamine 1-kinase was used to produce GlcNAc/GlcNTFA-1-phosphate from GlcNAc/GlcNTFA. N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12 MG1655 was used to produce UDP-GlcNAc/GlcNTFA from GlcNAc/GlcNTFA-1-phosphate. Inorganic pyrophosphatase from E. coli K12 MG1655 was used to hydrolyze pyrophosphate to accelerate the reaction. The above enzymes were expressed in E. coli BL21 (DE3) and purified, respectively, and finally mixed in one-pot bioreactor. The effects of reaction conditions on the production of UDP-GlcNAc and UDP-GlcNTFA were characterized. To avoid the substrate inhibition effect on the production of UDP-GlcNAc and UDP-GlcNTFA, the reaction was performed with fed batch of substrate. Under the optimized conditions, high production of UDP-GlcNAc (59.51 g/L) and UDP-GlcNTFA (46.54 g/L) were achieved in this three-enzyme one-pot system. The present work is promising to develop an efficient scalable process for the supply of UDP-monosaccharide donors for oligosaccharide synthesis.

Probing the roles of conserved residues in uridyltransferase domain of Escherichia coli K12 GlmU by site-directed mutagenesis

N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway. Our previous study demonstrated that the uridyltransferase domain of GlmU (tGlmU) exhibited a flexible substrate specificity, which could be further applied in unnatural sugar nucleotides preparation. However, the structural basis of tolerating variant substrates is still not clear. Herein, we further investigated the roles of several highly conserved amino acid residues involved in substrate binding and recognition by structure- and sequence-guided site-directed mutagenesis. Out of total 16 mutants designed, tGlmU Q76E mutant which had a novel catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc was identified. Furthermore, tGlmU Y103F and N169R mutants were also investigated to have enhanced uridyltransferase activities compared with wide-type tGlmU.

Biosynthesis of the carbamoylated D-gulosamine moiety of streptothricins: Involvement of a guanidino-N-glycosyltransferase and an N-acetyl-D-gulosamine deacetylase

Streptothricins (STNs) are atypical aminoglycosides containing a rare carbamoylated D-gulosamine (D-GulN) moiety, and the antimicrobial activity of STNs has been exploited for crop protection. Herein, the biosynthetic pathway of the carbamoylated D-GulN moiety was delineated. An N-acetyl-D-galactosamine is first attached to the streptolidine lactam by the glycosyltransferse StnG and then epimerized to N-acetyl-D-gulosamine by the putative epimerase StnJ. After carbamoylation by the carbamoyltransferase StnQ, N-acetyl-D-GulN is deacetylated by StnI to furnish the carbamoylated D-GulN moiety. In vitro studies characterized two novel enzymes: StnG is an unprecedented GT-A fold N-glycosyltransferase that glycosylates the imine nitrogen atom of guanidine, and StnI is the first reported N-acetyl-D-GulN deacetylase. The dynamic duo: Two novel enzymes, StnG and StnI, have been found to be involved in the biosynthetic pathway of the carbamoylated D-gulosamine moiety in streptothricins. StnG is a GT-A fold glycosyltransferase that catalyzes the unprecedented attachment of a sugar to the imine nitrogen atom of a guanidine group; StnI catalyzes the deacetylation of the N-acetyl-D-gulosamine moiety.

Enzymatic synthesis of nucleobase-modified UDP-sugars: Scope and limitations

Glucose-1-phosphate uridylyltransferase in conjunction with UDP-glucose pyrophosphorylase was found to catalyse the conversion of a range of 5-substituted UTP derivatives into the corresponding UDP-galactose derivatives in poor yield. Notably the 5-iodo derivative was not converted to UDP-sugar. In contrast, UDP-glucose pyrophosphorylase in conjunction with inorganic pyrophosphatase was particularly effective at converting 5-substituted UTP derivatives, including the iodo compound, into a range of gluco-configured 5-substituted UDP-sugar derivatives in good yields. Attempts to effect 4″-epimerization of these 5-substituted UDP-glucose with UDP-glucose 4″-epimerase from yeast were unsuccessful, while use of the corresponding enzyme from Erwinia amylovora resulted in efficient epimerization of only 5-iodo-UDP-Glc, but not the corresponding 5-aryl derivatives, to give 5-iodo-UDP-Gal. Given the established potential for Pd-mediated cross-coupling of 5-iodo-UDP-sugars, this provides convenient access to the galacto-configured 5-substituted-UDP-sugars from gluco-configured substrates and 5-iodo-UTP.

CHEMOENZYMATIC SYNTHESIS OF HEPARIN AND HEPARAN SULFATE ANALOGS

The present invention provides a one-pot multi-enzyme method for preparing UDP-sugars from simple sugar starting materials. The invention also provides a one-pot multi-enzyme method for preparing oligosaccharides from simple sugar starting materials.

Sequential one-pot enzymatic synthesis of oligo-N-acetyllactosamine and its multi-sialylated extensions

A simple and efficient protocol for the preparative-scale synthesis of various lengths of oligo-N-acetyllactosamine (oligo-LacNAc) and its multi-sialylated extensions is described. The strategy utilizes one thermophilic bacterial thymidylyltransferase (RmlA) coupled with corresponding sugar-1-phosphate kinases to generate two uridine diphosphate sugars, UDP-galactose and UDP-N-acetylglucosamine. By incorporating glycosyltransferases, oligo-LacNAcs and their sialylated analogs were synthesized. the Partner Organisations 2014.

A novel allosteric inhibitor of the uridine diphosphate N-acetylglucosamine pyrophosphorylase from Trypanosoma brucei

Uridine diphosphate N-acetylglucosamine pyrophosphorylase (UAP) catalyzes the final reaction in the biosynthesis of UDP-GlcNAc, an essential metabolite in many organisms including Trypanosoma brucei, the etiological agent of Human African Trypanosomiasis. High-throughput screening of recombinant T. brucei UAP identified a UTP-competitive inhibitor with selectivity over the human counterpart despite the high level of conservation of active site residues. Biophysical characterization of the UAP enzyme kinetics revealed that the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Structural characterization of the T. brucei UAP-inhibitor complex revealed that the inhibitor binds at an allosteric site absent in the human homologue that prevents the conformational rearrangement required to bind UTP. The identification of a selective inhibitory allosteric binding site in the parasite enzyme has therapeutic potential.