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Usage

Uses

Used in Pharmaceutical Industry:
Uridine diphosphate mannose is used as a key molecule for the synthesis of glycoconjugates, which are essential for various biological processes, including cell adhesion, signaling, and immune response. Its role in the biosynthesis of glycosaminoglycans makes it a valuable component in the development of drugs targeting extracellular matrix and connective tissue disorders.
Used in Biotechnology Industry:
Uridine diphosphate mannose is used as a substrate in various biosynthetic pathways, enabling the production of glycoproteins, glycolipids, and polysaccharides with specific functions. Its involvement in protein modification through the addition of mannose residues makes it a valuable tool in the engineering of proteins with improved stability and function.
Used in Research and Development:
Uridine diphosphate mannose is used as a research tool to study the role of glycosylation in various biological processes and diseases. Its involvement in the regulation of cellular functions and tissue integrity makes it an important molecule for understanding the underlying mechanisms of various pathological conditions and developing targeted therapies.
Used in Diagnostic Applications:
Uridine diphosphate mannose can be used as a biomarker for the assessment of glycosylation patterns in various diseases, such as cancer, inflammatory disorders, and genetic disorders affecting glycosylation pathways. Its role in the synthesis of glycoconjugates makes it a potential indicator of altered glycosylation patterns associated with disease progression and response to treatment.

InChI:InChI=1/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8-,9-,10+,11-,12+,13-,14?/m1/s1

Upstream product

• 6386-24-9 2,3,4,6-tetra-O-benzyl-D-galactopyranose 
• 67145-38-4 2,3,4,6-Tetra-O-benzyl-D-galactopyranosyl bromide 
• 10257-28-0 D-Galactose 
• 63-39-8 UTP 
• 27251-84-9 D-galactopyranose 1-phosphate 
• 58-98-0 UDP 
• 2280-44-6 D-Glucose 
• 59-56-3 mannose-1-phosphate 
• 58-96-8 uridine 
• 83-87-4 D-Mannose pentaacetate 
• 13242-53-0 acetobromomannose 
• 530-26-7 D-Mannose 

Downstream Products

• 4419-94-7 4-nitrophenyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside 
• 142925-37-9 4-nitrophenyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 330203-79-7 benzyl α-D-galactopyranosyl-(1->3)-β-D-galactopyranosyl-(1->)4-β-D-glucopyranoside 
• 27251-84-9 D-galactopyranose 1-phosphate 
• 47705-70-4 cyanidin 3-O-D-galactoside 
• 50986-17-9 delphinidin 3-O-galactoside 
• 73448-32-5 4-methylumbelliferyl β-D-galactopyranosyl-(1->4)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 115075-17-7 n-propyl 4-O-β-D-galactopyranosyl-β-D-glucopyranoside 
• 113960-55-7 bufalin-3-(β-D-glucoside) 
• 88901-39-7 mogroside IE₁ 

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.

One-Step Synthesis of Sugar Nucleotides

The chemical synthesis of sugar nucleotides requires a multistep procedure to ensure a selective reaction. Herein, sugar nucleotides were synthesized in one step using 2-chloro-1,3-dimethylimidazolinium chloride as the condensation reagent. The products were obtained in yields of 12-30%, and the yields were increased to 35-47% by the addition of a tuning reagent. NMR identification of the sugar nucleotides showed that mainly 1,2-trans-glycosides were present. The reported method represents a one-step route to sugar nucleotides from commercially available materials.

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.).

Efficient one-pot multienzyme synthesis of UDP-sugars using a promiscuous UDP-sugar pyrophosphorylase from Bifidobacterium longum (BLUSP)

A promiscuous UDP-sugar pyrophosphorylase (BLUSP) was cloned from Bifidobacterium longum strain ATCC55813 and used efficiently with a Pasteurella multocida inorganic pyrophosphatase (PmPpA) with or without a monosaccharide 1-kinase for one-pot multienzyme synthesis of UDP-galactose, UDP-glucose, UDP-mannose, and their derivatives. Further chemical diversification of a UDP-mannose derivative resulted in the formation of UDP-N-acetylmannosamine. The Royal Society of Chemistry 2012.

Leishmania UDP-sugar pyrophosphorylase: The missing link in galactose salvage?

The Leishmania parasite glycocalyx is rich in galactose-containing glycoconjugates that are synthesized by specific glycosyltransferases that use UDP-galactose as a glycosyl donor. UDP-galactose biosynthesis is thought to be predominantly a de novo process involving epimerization of the abundant nucleotide sugar UDP-glucose by the UDP-glucose 4-epimerase, although galactose salvage from the environment has been demonstrated for Leishmania major. Here, we present the characterization of an L. major UDP-sugar pyrophosphorylase able to reversibly activate galactose 1-phosphate into UDP-galactose thus proving the existence of the Isselbacher salvage pathway in this parasite. The ordered bisubstrate mechanism and high affinity of the enzyme for UTP seem to favor the synthesis of nucleotide sugar rather than their pyrophosphorolysis. Although L. major UDP-sugar pyrophosphorylase preferentially activates galactose 1-phosphate and glucose 1-phosphate, the enzyme is able to act on a variety of hexose 1-phosphates as well as pentose 1-phosphates but not hexosamine 1-phosphates and hence presents a broad in vitro specificity. The newly identified enzyme exhibits a low but significant homology with UDP-glucose pyrophosphorylases and conserved in particular is the pyrophosphorylase consensus sequence and residues involved in nucleotide and phosphate binding. Saturation transfer difference NMR spectroscopy experiments confirm the importance of these moieties for substrate binding. The described leishmanial enzyme is closely related to plant UDP-sugar pyrophosphorylases and presents a similar substrate specificity suggesting their common origin.

Phosphomannose isomerase/GDP-mannose pyrophosphorylase from Pyrococcus furiosus: A thermostable biocatalyst for the synthesis of guanidinediphosphate- activated and mannose-containing sugar nucleotides

Herein we present an analysis of the chemical function of a recombinant bifunctional phosphomannose isomerase/GDP-mannose pyrophosphorylase (manC) from Pyrococcus furiosus DSM 3638 and its use in the synthesis of guanidinediphospho-hexoses and a range of

Sugar nucleotide recognition by Klebsiella pneumoniae UDP-d-galactopyranose mutase: Fluorinated substrates, kinetics and equilibria

A series of selectively fluorinated and other substituted UDP-d-galactose derivatives have been evaluated as substrates for Klebsiella pneumoniae UDP-d-galactopyranose mutase. This enzyme, which catalyses the interconversion of the pyranose and furanose f

Stereoselective chemical synthesis of sugar nucleotides via direct displacement of acylated glycosyl bromides

Figure presented The use of Leloir glycosyltransferases to prepare biologically relevant oligosaccharides and glycoconjugates requires access to sugar nucleoside diphosphates, which are notoriously difficult to efficiently synthesize and purify. We report a novel stereoselective route to UDP- and GDPα-D-mannose as well as UDP- and GDP-β-L-fucose via direct displacement of acylated glycosyl bromides with nucleoside 5′- diphosphates.

Structure-activity relationship of uridine 5′-diphosphoglucose analogues as agonists of the human P2Y14 receptor

UDP-glucose (UDPG) and derivatives are naturally occurring agonists of the Gi protein-coupled P2Y14 receptor, which occurs in the immune system. We synthesized and characterized pharmacologically novel analogues of UDPG modified on the nucleobase, ribose, and glucose moieties, as the basis for designing novel ligands in conjunction with modeling. The recombinant human P2Y14 receptor expressed in COS-7 cells was coupled to phospholipase C through an engineered Gα-q/i protein. Most modifications of the uracil or ribose moieties abolished activity; this is among the least permissive P2Y receptors. However, a 2-thiouracil modification in 15 (EC50 49 ± 2 nM) enhanced the potency of UDPG (but not UDP-glucuronic acid) by 7-fold. 4-Thio analogue 13 was equipotent to UDPG, but S-alkylation was detrimental. Compound 15 was docked in a rhodposin-based receptor homology model, which correctly predicted potent agonism of UDP-fructose, UDP-mannose, and UDP-inositol. The hexose moiety of UDPG interacts with multiple H-bonding and charged residues and provides a fertile region for agonist modification.

Exploiting nucleotidylyltransferases to prepare sugar nucleotides

(Graph Presented) Enzymatic approaches to prepare sugar nucleotides are gaining in importance and offer several advantages over chemical synthesis including high yields and stereospecificity. We report the cloning, expression, and purification of two new wild-type thymidylyltransferases and observed catalysis with a wide variety of substrates. Significant product inhibition was not observed with the enzymes studied over a 24 h period, enabling the efficient preparation of 15 sugar nucleotides, clearly demonstrating the synthetic utility of these biocatalysts.