38-57-3

Basic information

• Product Name: [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3R,4S,5R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl dihydrogen diphosphate (non-preferred name)
• CAS NO: 38-57-3
• Molecular Formula: C₁₄H₂₂N₂O₁₆P₂
• Molecular Weight: 536.2758
• Mol File: 38-57-3.mol

Chemical Properties

• Density: 1.96g/cm³
• Refractive Index: 1.665
• CAS DataBase Reference: [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3R,4S,5R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl dihydrogen diphosphate (non-preferred name)(CAS DataBase Reference)
• NIST Chemistry Reference: [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3R,4S,5R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl dihydrogen diphosphate (non-preferred name)(38-57-3)
• EPA Substance Registry System: [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3R,4S,5R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl dihydrogen diphosphate (non-preferred name)(38-57-3)

Safety Data

• Hazardous Substances Data: 38-57-3(Hazardous Substances Data)

Upstream product

• 2616-64-0 UDP-glucuronic acid 
• 25799-81-9 α-D-xylose 1-phosphate, free acid 
• 25747-29-9 UDP-α-D-4-ketoxylose 
• 2280-44-6 D-Glucose 
• 133-89-1 UDP-glucose 
• 63-39-8 UTP 
• 50574-25-9 O¹-Phosphono-β-L-arabinopyranose 
• 87-72-9 L-(+)-arabinose 
• 32166-73-7 per-O-trimethylsilyl-L-arabinose 
• 18039-26-4 2,3,4-tri-O-benzyloxy-L-arabinopyranose 
• 58-97-9 5'-Uridylic Acid 
• 56428-57-0 uridine 5’-monophosphate-imidazole 

Downstream Products

• 84687-42-3 astragaloside III 

Relevant articles and documents

Practical preparation of UDP-apiose and its applications for studying apiosyltransferase

UDP-apiose, a donor substrate of apiosyltransferases, is labile because of its intramolecular self-cyclization ability, resulting in the formation of apiofuranosyl-1,2-cyclic phosphate. Therefore, stabilization of UDP-apiose is indispensable for its availability and identifying and characterizing the apiosyltransferases involved in the biosynthesis of apiosylated sugar chains and glycosides. Here, we established a method for stabilizing UDP-apiose using bulky cations as counter ions. Bulky cations such as triethylamine effectively suppressed the degradation of UDP-apiose in solution. The half-life of UDP-apiose was increased to 48.1 ± 2.4 h at pH 6.0 and 25 °C using triethylamine as a counter cation. UDP-apiose coordinated with a counter cation enabled long-term storage under freezing conditions. UDP-apiose was utilized as a donor substrate for apigenin 7-O-β-D-glucoside apiosyltransferase to produce the apiosylated glycoside apiin. This apiosyltransferase assay will be useful for identifying genes encoding apiosyltransferases.

Isotope Probing of the UDP-Apiose/UDP-Xylose Synthase Reaction: Evidence of a Mechanism via a Coupled Oxidation and Aldol Cleavage

The C-branched sugar d-apiose (Api) is essential for plant cell-wall development. An enzyme-catalyzed decarboxylation/pyranoside ring-contraction reaction leads from UDP-α-d-glucuronic acid (UDP-GlcA) to the Api precursor UDP-α-d-apiose (UDP-Api). We examined the mechanism of UDP-Api/UDP-α-d-xylose synthase (UAXS) with site-selectively2H-labeled and deoxygenated substrates. The analogue UDP-2-deoxy-GlcA, which prevents C-2/C-3 aldol cleavage as the plausible initiating step of pyranoside-to-furanoside conversion, did not give the corresponding Api product. Kinetic isotope effects (KIEs) support an UAXS mechanism in which substrate oxidation by enzyme-NAD+and retro-aldol sugar ring-opening occur coupled in a single rate-limiting step leading to decarboxylation. Rearrangement and ring-contracting aldol addition in an open-chain intermediate then give the UDP-Api aldehyde, which is intercepted via reduction by enzyme-NADH.

Enzymatic redox cascade for one-pot synthesis of Uridine 5'-Diphosphate xylose from Uridine 5'-Diphosphate glucose

Synthetic ways towards uridine 5'-diphosphate (UDP)-xylose are scarce and not well established, although this compound plays an important role in the glycobiology of various organisms and cell types. We show here how UDP-glucose 6-dehydrogenase (hUGDH) and UDP-xylose synthase 1 (hUXS) from Homo sapiens can be used for the efficient production of pure UDP-a-xylose from UDPglucose. In a mimic of the natural biosynthetic route, UDP-glucose is converted to UDP-glucuronic acid by hUGDH, followed by subsequent formation of UDP-xylose by hUXS. The nicotinamide adenine dinucleotide (NAD+) required in the hUGDH reaction is continuously regenerated in a three-step chemoenzymatic cascade. In the first step, reduced NAD+ (NADH) is recycled by xylose reductase from Candida tenuis via reduction of 9,10-phenanthrenequinone (PQ). Radical chemical re-oxidation of this mediator in the second step reduces molecular oxygen to hydrogen peroxide (H2O2) that is cleaved by bovine liver catalase in the last step. A comprehensive analysis of the coupled chemo-enzymatic reactions revealed pronounced inhibition of hUGDH by NADH and UDP-xylose as well as an adequate oxygen supply for PQ re-oxidation as major bottlenecks of effective performance of the overall multi-step reaction system. Net oxidation of UDP-glucose to UDPxylose by hydrogen peroxide (H2O2) could thus be achieved when using an in situ oxygen supply through periodic external feed of H2O2 during the reaction. Engineering of the interrelated reaction parameters finally enabled production of 19.5 mM (10.5 gL-1) UDP-a-xylose. After two-step chromatographic purification the compound was obtained in high purity (>98%) and good overall yield (46%). The results provide a strong case for application of multi-step redox cascades in the synthesis of nucleotide sugar products.

Identification of a bifunctional UDP-4-keto-pentose/UDP-xylose synthase in the plant pathogenic bacterium Ralstonia solanacearum strain GMI1000, a distinct member of the 4,6-dehydratase and decarboxylase family

The UDP-sugar interconverting enzymes involved in UDP-GlcA metabolism are well described in eukaryotes but less is known in prokaryotes. Here we identify and characterize a gene (RsU4kpxs) from Ralstonia solanacearum str. GMI1000, which encodes a dual function enzyme not previously described. One activity is to decarboxylate UDP-glucuronic acid to UDP-β-L-threo-pentopyranosyl- 4″-ulose in the presence of NAD+. The second activity converts UDP-β-L-threo-pentopyranosyl-4″-ulose and NADH to UDP-xylose and NAD+, albeit at a lower rate. Our data also suggest that following decarboxylation, there is stereospecific protonation at the C5 pro-R position. The identification of the R. solanacearum enzyme enables us to propose that the ancestral enzyme of UDP-xylose synthase and UDP-apiose/UDP-xylose synthase was diverged to two distinct enzymatic activities in early bacteria. This separation gave rise to the current UDP-xylose synthase in animal, fungus, and plant as well as to the plant Uaxs and bacterial ArnA and U4kpxs homologs.

Chemical synthesis of uridine 5′-diphospho-α-D-xylopyranose

Uridine 5′-diphospho-α-d-xylopyranose, which donates d-xylose during glycoconjugate biosynthesis, was chemically synthesized from α-d-xylose 1-phosphate and uridine 5′-monophosphoimidazolide.

Rapid conversion of unprotected galactose analogs to their UDP-derivatives for use in the chemoenzymatic synthesis of unnatural oligosaccharides

The rapid conversion of D-galactose, its 2-deoxy, 3-deoxy, 4-deoxy and 6-deoxy derivatives and L-arabinose to their UDP-derivatives (2-7) is described. The procedure involves the in situ preparation of the per-O-trimethylsilylated glycopyranosyl iodides and their direct reaction with UDP. All six sugar nucleotides were active as substrates for β(1→4)-galactosyltransferase and were used to enzymatically prepare N-acetyllactosamine (8) and five of its analogs (9-13).