30174-43-7

Basic information

• Product Name: uridine 5'-(beta-rhamnopyranosyl diphosphate)
• Synonyms: uridine 5'-(beta-rhamnopyranosyl diphosphate);UDP-L-Gal.2NH 3
• CAS NO: 30174-43-7
• Molecular Formula: C15H24 N2 O16 P2
• Molecular Weight: 550.3024
• Mol File: 30174-43-7.mol
• Article Data: 12

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.959g/cm³
• Refractive Index: 1.671
• CAS DataBase Reference: uridine 5'-(beta-rhamnopyranosyl diphosphate)(CAS DataBase Reference)
• NIST Chemistry Reference: uridine 5'-(beta-rhamnopyranosyl diphosphate)(30174-43-7)
• EPA Substance Registry System: uridine 5'-(beta-rhamnopyranosyl diphosphate)(30174-43-7)

Safety Data

• Hazardous Substances Data: 30174-43-7(Hazardous Substances Data)

Usage

General Description

Uridine 5'-(beta-rhamnopyranosyl diphosphate) is a chemical compound that is involved in the biosynthesis of cell wall polysaccharides in bacteria. It is a nucleotide sugar that serves as a precursor for the synthesis of rhamnose, a sugar found in the cell walls of some bacteria. uridine 5'-(beta-rhamnopyranosyl diphosphate) plays a crucial role in the formation of the bacterial cell wall, which is essential for protecting the cell from its environment and maintaining its structural integrity. Uridine 5'-(beta-rhamnopyranosyl diphosphate) is a key component in the complex biochemical pathways that regulate cell wall synthesis in bacteria and is therefore an important target for understanding and potentially manipulating bacterial cell wall biosynthesis.

InChI:InChI=1/C15H24N2O16P2/c1-4-6(19)7(20)8(21)11(30-4)13(32-35(28,29)33-34(25,26)27)12-9(22)10(23)14(31-12)17-3-2-5(18)16-15(17)24/h2-4,6-14,19-23H,1H3,(H,28,29)(H,16,18,24)(H2,25,26,27)/t4-,6-,7+,8+,9-,10+,11?,12-,13?,14+/m0/s1

Upstream product

• 128473-03-0 dibenzyl 2,3,4-tri-O-acetyl-α-L-fucopyranosyl phosphate 
• 140223-15-0 (3S,4R,5R,6S)-6-methyltetrahydro-2H-pyran-2,3,4,5-tetrayl tetrabenzoate 
• 131897-73-9 2,3,4-tri-O-benzoyl-α-L-fucopyranosyl bromide 
• 16562-59-7 β-L-Fucopyranosyl phosphate 
• 63-39-8 UTP 
• 73-34-7 D-Fucose 
• 1476-50-2 uridine 5'-triphosphate trisodium salt 
• 157365-62-3 2,3,4-tri-O-acetyl-6-deoxy-α-D-galactopyranose 
• 81276-27-9 Gal6deoxy-1-P 
• 51921-33-6 1,2,3,4-tetra-O-acetyl-D-fucopyranose 
• 5158-64-5 2,3,4-tri-O-acetyl-D-fucopyranosyl bromide 
• 153448-93-2 2,3,4-tri-O-acetyl-6-deoxy-α-D-galactopyranosyl 1-phosphate dibenzyl ester 
• 28915-80-2 2,3,4-tri-O-acetyl-6-deoxy-D-galactopyranose 

Relevant articles and documents

Expanded investigations of the aglycon promiscuity and catalysis characteristic of flavonol 3-: O -rhamnosyltransferase AtUGT78D1 from Arabidopsis thaliana

Rhamnosides usually possess better bioavailabilities and improved solubilities compared with their aglycons and are a major source of bioactive natural products. However, biosynthesis of rhamnosides is hindered by the commercially expensive UDP-rhamnose (UDP-Rha) donor and a lack of universal rhamnosyltransferases. In the present study, an efficient UDP-Rha production system via a two-step enzymatic reactions using UDP-glucose (UDP-Glc) as a substrate was constructed. Extensive in vitro enzymatic assays and preparative reactions using the obtained UDP-Rha/UDP-Glc highlighted the robust glycosylation promiscuity of the reported rhamnosyltransferase AtUGT78D1. Based on HPLC-UV and HR-MS analyses, 30 of the tested aromatic compounds belonging to 7 structural types, including flavonoids, flavonoid glycosides, phenylethyl chromones, benzophenones, coumarins, lignanoids, and anthraquinones, were accepted by AtUGT78D1 to conduct the corresponding rhamnosylation and/or glucosylation with one or more glycosyl substitutions at different positions. Further preparative reactions expanded the catalytic characteristic of AtUGT78D1 since it can catalyse the rhamnosylation at the 3-OH position of the flavonols, glucosylation at the 7-OH position of the flavone baicalein, and multiple hydroxyl substitutions for diverse types of aromatics. Interestingly, a unique reversible catalysis activity of AtUGT78D1 was observed, and it has been effectively used in one-pot rhamnosylation of the desired rhamnoside. The enzymatic rhamnosylations of diverse "drug-like" scaffolds as well as bidirectional catalysis for one-pot rhamnosylations by plant rhamnosyltransferase were rarely reported before, which indicated that AtUGT78D1 was expected to be a universal and effective tool for chemo-enzymatic synthesis of diverse bioactive rhamnosylated derivatives for drug discovery.

One-pot three-enzyme synthesis of UDP-Glc, UDP-Gal, and their derivatives

A UTP-glucose-1-phosphate uridylyltransferase (SpGalU) and a galactokinase (SpGalK) were cloned from Streptococcus pneumoniae TIGR4 and were successfully used to synthesize UDP-galactose (UDP-Gal), UDP-glucose (UDP-Glc), and their derivatives in an efficient one-pot reaction system. The reaction conditions for the one-pot multi-enzyme synthesis were optimized and nine UDP-Glc/Gal derivatives were synthesized. Using this system, six unnatural UDP-Gal derivatives, including UDP-2-deoxy-Galactose and UDP-GalN3 which were not accepted by other approach, can be synthesized efficiently in a one pot fashion. More interestingly, this is the first time it has been reported that UDP-Glc can be synthesized in a simpler one-pot three-enzyme synthesis reaction system.

Unusually broad substrate tolerance of a heat-stable archaeal sugar nucleotidyltransferase for the synthesis of sugar nucleotides

Herein, we report the first cloning, recombinant expression, and synthetic utility of a sugar nucleotidyltransferase from any archaeal source and demonstrate by an electrospray ionization mass spectrometry (ESI-MS)-based assay its unusual tolerance of heat, pH, and sugar substrates. The metalion-dependent enzyme from Pyrococcus furiosus DSM 3638 showed a relatively high degree of acceptance of glucose-1-phosphate (Glc1P), mannose-1-phosphate (Man1P), galactose-1-phosphate (Gal1P), fucose-1-phosphate, glucosamine-1-phosphate, galactosamine-1-phosphate, and N-acetylglucosamine-1-phosphate with uridine and deoxythymidine triphosphate (UTP and dTTP, respectively). The apparent Michaelis constants for Glc1P, Man1P, and Gal1P are 13.0 ± 0.7, 15 ± 1, and 22 ± 2 μM, respectively, with corresponding turnover numbers of 2.08, 1.65, and 1.32 s-1, respectively. An initial velocity study indicated an ordered bi-bi catalytic mechanism for this enzyme. The temperature stability and inherently broad substrate tolerance of this archaeal enzyme promise an effective reagent for the rapid chemoenzymatic synthesis of a range of natural and unnatural sugar nucleotides for in vitro glycosylation studies and highlight the potential of archaea as a source of new enzymes for synthesis.