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
• Article Data: 35

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

General Description

Uridine diphosphate N-acetyl-D-glucosamine, [glucosamine-14C(U)] is a biochemical compound used in metabolic studies to investigate the biosynthesis and degradation of complex carbohydrates. It is a nucleotide sugar that serves as a substrate for various enzymes involved in glycosylation processes, including the synthesis of glycoproteins, glycolipids, and proteoglycans. The radioactive isotope 14C in the compound allows for tracing and quantifying the incorporation of glucosamine into various biological molecules in cells and tissues. URIDINE DIPHOSPHATE N-ACETYL-D-GLUCOSAMINE, [GLUCOSAMINE-14C(U)] is instrumental in understanding the role of N-acetyl-D-glucosamine in cellular processes and its potential uses in therapeutic applications for conditions such as osteoarthritis and inflammatory disorders.

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

• 18191-20-3 N-acetyl-D-glucosamine-6-phosphate 
• 28446-21-1 N-acetylglucosamine-1-phosphate 
• 63-39-8 UTP 
• 97604-58-5 2-azido-2-deoxy-D-mannopyranose 
• 1366133-51-8 UDP-ManN 
• 75-36-5 acetyl chloride 
• 1363386-22-4 uridine 5'-diphospho-2-azido-2-deoxy-α-D-mannopyranoside 
• 72-87-7 N-acetyl-D-galactosamine 
• 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 
• 436853-00-8 C₂₁H₃₁NO₁₁ 
• 1307843-25-9 C₃₈H₅₁F₇N₂O₂₁ 
• 24758-79-0 UDP-N-acetyl-D-glucosaminuronic acid 
• 16124-22-4 UDP-N-acetylmuramyl-L-alanyl-γ-D-glutamyl-m-diaminopimelyl-D-alanyl-D-alanine 
• 27208-79-3 2-amino-2-deoxy-α,α-D-trehalose 

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%.

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.

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.