27416-86-0

Basic information

• Product Name: POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000*
• Synonyms: POLYURIDYLIC ACID POT. SALT, LYOPH., MR ;polyu;polyuridylic acid pot. salt
• CAS NO: 27416-86-0
• Molecular Formula: C9H13N2O9P
• Molecular Weight: 324.181281
• Product Categories: Biochemicals and Reagents;Biomaterials;Materials Science;Nucleosides;Nucleotides;Oligonucleotide Polymers and Copolymers;Oligonucleotides;Synthetic Oligonucleotides and Related Reagents
• Mol File: 27416-86-0.mol
• Article Data: 67

Chemical Properties

• Melting Point: 28 °C
• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000*(CAS DataBase Reference)
• NIST Chemistry Reference: POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000*(27416-86-0)
• EPA Substance Registry System: POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000*(27416-86-0)

Safety Data

• Hazard Codes: Xn
• Statements: 42/43
• Safety Statements: 22-36/37
• WGK Germany: 3
• F: 3-10-21
• Hazardous Substances Data: 27416-86-0(Hazardous Substances Data)

Usage

Description

POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 is a homopolymer of uridine, which is a single-stranded RNA (ssRNA) model compound. It is commonly used in scientific research to study processes that are dependent upon ssRNA regulation, such as Toll-like receptor regulation. POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 is lyophilized, which means it has been freeze-dried to remove water, and has a molecular weight of less than 900,000.

Uses

Used in Research Applications:
POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 is used as a single-stranded RNA model compound for studying ssRNA regulation processes. It is particularly useful in comparing with other ssRNA model oligonucleotides such as Poly(I) and Poly(C) to understand the mechanisms of Toll-like receptor regulation and other ssRNA-dependent processes.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 can be used as a component in the development of drugs targeting ssRNA regulation pathways. By understanding the interactions between this compound and other biological molecules, researchers can potentially develop new therapeutic strategies for various diseases.
Used in Diagnostics:
POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 can also be employed in the development of diagnostic tools that rely on the detection or manipulation of ssRNA molecules. This could include the creation of assays or tests that help identify specific RNA signatures associated with certain diseases or conditions.
Used in Biochemical Research:
In the field of biochemistry, POLYURIDYLIC ACID POT. SALT, LYOPH., MR <900000 can be utilized to study the structure, function, and interactions of RNA molecules. This knowledge can contribute to a better understanding of RNA biology and its role in cellular processes, which may lead to the discovery of new targets for therapeutic intervention.

InChI:InChI=1/C9H13N2O9P/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(20-8)3-19-21(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1

Upstream product

• 55728-64-8 O^2',O^3'-isopropylidene-[5']uridylic acid 
• 58-96-8 uridine 
• 97-55-2 5-phosphoribosyl-1-pyrophosphate 
• 66-22-8 uracil 
• 3257-71-4 (R)-2',3'-O-benzylideneuridine 
• 65-86-1 orotic acid 
• 362-43-6 2',3'-O-isopropylideneuridine 
• 7075-11-8 cytosine arabinoside-5'-monophosphate 
• 1029916-52-6 Ara-C triphosphate 
• 24514-44-1 5'-amino-5'-deoxyuridine 
• 63-39-8 UTP 
• 1313724-78-5 bis-2',3'-O-alanyl-UMP 
• 112677-94-8 Phosphoric acid diallyl ester (3aR,4R,6R,6aR)-6-(2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethyl ester 
• 81788-35-4 uridine 5'-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl phosphoric acid) 

Downstream Products

• 56428-57-0 uridine 5’-monophosphate-imidazole 
• 59985-21-6 _P¹,_P⁴-di(uridine-5')-tetraphosphate 
• 24514-44-1 5'-amino-5'-deoxyuridine 
• 1263057-00-6 C₂₇H₄₇N₆O₁₉P 
• 34198-43-1 5-Iodo-UTP 
• 50-99-7 D-glucose 
• 528-04-1 uridine-5'-diphospho-N-acetyl-D-galactosamine 
• 3616-06-6 UDP-xylose 
• 65331-79-5 Ap2U 
• 17479-06-0 uridine 5'-(2-amino-2-deoxy-α-D-galactopyranosyl diphosphate) 
• 5746-18-9 1-methyl-4-carboxypyridinium chloride 
• 2149-79-3 5-Brom-uridin-5'-phosphat 
• 4004-57-3 uridine 3',5'-cyclic monophosphate 
• 59237-85-3 UMP-DMPA 

Relevant articles and documents

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On the observation of discrete fluorine NMR spectra for uridine 5'-β,γ-fluoromethylenetriphosphate diastereomers at basic pH

Jakeman et al. recently reported the inability to distinguish the diastereomers of uridine 5'-β,γ-fluoromethylenetriphosphate (β,γ-CHF-UTP, 1) by 19F NMR under conditions we previously prescribed for the resolution of the corresponding β,γ-CHF-

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Rate enhancements brought about by uridine nucleotides in the reduction of NAD+ at the active site of UDP-galactose 4-epimerase

UDP-galactose 4-epimerase catalyzes the interconversion of UDP-galactose and UDP glucose. In the course of the reaction, the galacto- and glucopyranosyl rings undergo reversible oxidation to the 4-keto- glucopyranosyl ring by reaction with the enzyme-bound NAD+. The UDP-moiety of a substrate participates in catalysis by inducing a conformational change in the enzyme that enhances the chemical reactivity of NAD+ toward reducing agents. This is modeled by UMP-dependent reductive inactivation of the epimerase-NAD+ complex by various sugars as well as by borohydrides. The present work shows that UDP also activates the reduction of epimerase-bound NAD+. Furthermore, the reduction of epimerase-NAD+ by glucose at a very slow rate can be observed under anaerobic conditions in the absence of a uridine nucleotide. Comparisons of the second order rate constants for reduction of epimerase-NAD+ by glucose in the presence and absence of uridine nucleotides have allowed the magnitude of the rate enhancements brought about by UMP and UDP to be estimated. The rate enhancements by UMP and UDP correspond to decreases of 5.7 and 4.1 kcal mol-1, respectively, in the activation energy. A decrease of 4.0 kcal mol-1 in the activation energy for reduction by NaBH3CN was brought about by UMP-binding. The maximum increases in the reduction potential of epimerase-NAD+ induced by UMP- and UDP-binding are estimated to be 120 and 90 mV, respectively. The results are well correlated with the perturbations of the nicotinamide-13C NMR chemical shifts brought about by uridine nucleotides (Burke, J. R., and Frey, P. A. (1993) Biochemistry 32, 13220-12230). (C) 2000 Academic Press.

Conformational changes in orotidine 5′-monophosphate decarboxylase: "remote" residues that stabilize the active conformation

The structural factors responsible for the extraordinary rate enhancement (～1017) of the reaction catalyzed by orotidine 5′-monophosphate decarboxylase (OMPDC) have not been defined. Catalysis requires a conformational change that closes an active site loop and "clamps" the orotate base proximal to hydrogen-bonded networks that destabilize the substrate and stabilize the intermediate. In the OMPDC from Methanobacter thermoautotrophicus, a "remote" structurally conserved cluster of hydrophobic residues that includes Val 182 in the active site loop is assembled in the closed, catalytically active conformation. Substitution of these residues with Ala decreases kcat/Km with a minimal effect on kcat, providing evidence that the cluster stabilizes the closed conformation. The intrinsic binding energies of the 5′-phosphate group of orotidine 5′-monophosphate for the mutant enzymes are similar to that for the wild type, supporting this conclusion.

Product deuterium isotope effects for orotidine 5′-monophosphate decarboxylase: Effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate

A product deuterium isotope effect (PIE) of 1.0 was determined as the ratio of the yields of [6-1H]-uridine 5′-monophosphate (50%) and [6-2H]-uridine 5′-monophosphate (50%) from the decarboxylation of orotidine 5′-monophosphate (OMP) in 50/50 (v/v) HOH/DOD catalyzed by orotidine 5′-monophosphate decarboxylase (OMPDC) from Saccharomyces cerevisiae, Methanothermobacter thermautotrophicus, and Escherichia coli. This unitary PIE eliminates a proposed mechanism for enzyme-catalyzed decarboxylation in which proton transfer from Lys-93 to C-6 of OMP provides electrophilic push to the loss of CO2 in a concerted reaction. We propose that the complete lack of selectivity for the reaction of solvent H and D, which is implied by the value of PIE = 1.0, is enforced by restricted C-N bond rotation of the -CH2-NL3+ group of the side chain of Lys-93. A smaller PIE of 0.93 was determined as the ratio of the product yields for OMPDC-catalyzed decarboxylation of 5-fluoroorotidine 5′-monophosphate (5-FOMP) in 50/50 (v/v) HOH/DOD. Mutations on the following important active-site residues of OMPDC from S. cerevisiae have no effect on the PIE on OMPDC-catalyzed decarboxylation of OMP or decarboxylation of 5-FOMP: R235A, Y217A, Q215A, S124A, and S154A/Q215A.

Evidence for a stepwise mechanism of OMP decarboxylase [16]

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Kinetic and NMR spectroscopic study of the chemical stability and reaction pathways of sugar nucleotides

The alkaline cleavage of two types of sugar nucleotides has been studied by 1H and 31P NMR in order to obtain information on the stability and decomposition pathways in aqueous solutions under alkaline conditions. The reaction of glucose 1-UDP is straightforward, and products are easy to identify. The results obtained with ribose 5-UDP and ribose 5-phosphate reveal, in contrast, a more complex reaction system than expected, and the identification of individual intermediate species was not possible. Even though definite proof for the mechanisms previously proposed could not be obtained, all the spectroscopic evidence is consistent with them. Results also emphasise the significant effect of conditions, pH, ionic strength, and temperature, on the reactivity under chemical conditions.

Enzymatic Production of Non-Natural Nucleoside-5′-Monophosphates by a Thermostable Uracil Phosphoribosyltransferase

The use of enzymes as biocatalysts applied to synthesis of modified nucleoside-5′-monophosphates (NMPs) is an interesting alternative to traditional multistep chemical methods which offers several advantages, such as stereo-, regio-, and enantioselectivity, simple downstream processing, and mild reaction conditions. Herein we report the recombinant expression, production, and purification of uracil phosphoribosyltransferase from Thermus themophilus HB8 (TtUPRT). The structure of TtUPRT has been determined by protein crystallography, and its substrate specificity and biochemical characteristics have been analyzed, providing new structural insights into the substrate-binding mode. Biochemical characterization of the recombinant protein indicates that the enzyme is a homotetramer, with activity and stability across a broad range of temperatures (50–80 °C), pH (5.5–9) and ionic strength (0–500 mm NaCl). Surprisingly, TtUPRT is able to recognize several 5 and 6-substituted pyrimidines as substrates. These experimental results suggest TtUPRT could be a valuable biocatalyst for the synthesis of modified NMPs.