50722-58-2

Basic information

• Product Name: UDP-galacturonic acid
• Synonyms: UDP-galacturonic acid
• CAS NO: 50722-58-2
• Molecular Formula: C₁₅H₂₂N₂O₁₈P₂
• Molecular Weight: 580.285302
• Mol File: 50722-58-2.mol

Chemical Properties

• Appearance: /
• Density: 2.05g/cm³
• Refractive Index: 1.684
• CAS DataBase Reference: UDP-galacturonic acid(CAS DataBase Reference)
• NIST Chemistry Reference: UDP-galacturonic acid(50722-58-2)
• EPA Substance Registry System: UDP-galacturonic acid(50722-58-2)

Safety Data

• Hazardous Substances Data: 50722-58-2(Hazardous Substances Data)

Usage

InChI:InChI=1/C15H22N2O18P2/c18-5-1-2-17(15(26)16-5)12-7(20)6(19)4(32-12)3-31-37(30,35-36(27,28)29)34-10-8(21)11(13(23)24)33-14(25)9(10)22/h1-2,4,6-12,14,19-22,25H,3H2,(H,23,24)(H,16,18,26)(H2,27,28,29)/t4-,6-,7-,8-,9-,10+,11+,12-,14+,37?/m1/s1

Upstream product

• 6294-16-2 D-galacturonic acid 
• 63-39-8 UTP 
• 489-91-8 D-galacturonic acid 
• 59-56-3 α-D-glucopyranosyl-1-phosphate 
• 2616-64-0 UDP-glucuronic acid 
• 133-89-1 UDP-glucose 

Downstream Products

• 1448012-77-8 C₂₆H₃₁F₃N₂O₂₀ 
• 1448012-76-7 GlcA-β-1,4-GlcNAc-α-1,4-GlcA-pNP 
• 58-98-0 UDP 
• 249938-52-1 kaempferol-7-O-β-D-glucuronide 
• 22688-78-4 kaempferol 3-O-β-D-glucuronide 
• 463955-79-5 Galangin O₃-glucuronide 
• 463955-75-1 Galangin O₇-glucuronide 
• 1242087-66-6 Resokaempferol 3-glucuronide 
• 1242087-79-1 C₂₁H₁₈O₁₁ 
• 1242087-61-1 3,7-Dihydroxyflavone 3-glucuronide 
• 1242087-71-3 C₂₁H₁₈O₁₀ 
• 81256-81-7 1'-Hydroxymidazolam glucuronide 
• 81256-82-8 4-Hydroxymidazolam O-glucuronide 
• 123685-24-5 phloretin-2′-O-β-D-glucuronide 

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%.

Mechanistic characterization of UDP-glucuronic acid 4-epimerase

UDP-glucuronic acid (UDP-GlcA) is a central precursor in sugar nucleotide biosynthesis and common substrate for C4-epimerases and decarboxylases releasing UDP-galacturonic acid (UDP-GalA) and UDP-pentose products, respectively. Despite the different reactions catalyzed, the enzymes are believed to share mechanistic analogy rooted in their joint membership to the short-chain dehydrogenase/reductase (SDR) protein superfamily: Oxidation at the substrate C4 by enzyme-bound NAD+ initiates the catalytic pathway. Here, we present mechanistic characterization of the C4-epimerization of UDP-GlcA, which in comparison with the corresponding decarboxylation has been largely unexplored. The UDP-GlcA 4-epimerase from Bacillus cereus functions as a homodimer and contains one NAD+/subunit (kcat?=?0.25?±?0.01?s?1). The epimerization of UDP-GlcA proceeds via hydride transfer from and to the substrate’s C4 while retaining the enzyme-bound cofactor in its oxidized form (≥?97%) at steady state and without trace of decarboxylation. The kcat for UDP-GlcA conversion shows a kinetic isotope effect of 2.0 (±0.1) derived from substrate deuteration at C4. The proposed enzymatic mechanism involves a transient UDP-4-keto-hexose-uronic acid intermediate whose formation is rate-limiting overall, and is governed by a conformational step before hydride abstraction from UDP-GlcA. Precise positioning of the substrate in a kinetically slow binding step may be important for the epimerase to establish stereo-electronic constraints in which decarboxylation of the labile β-keto acid species is prevented effectively. Mutagenesis and pH studies implicate the conserved Tyr149 as the catalytic base for substrate oxidation and show its involvement in the substrate positioning step. Collectively, this study suggests that based on overall mechanistic analogy, stereo-electronic control may be a distinguishing feature of catalysis by SDR-type epimerases and decarboxylases active on UDP-GlcA.

Comparing substrate specificity of two UDP-sugar pyrophosphorylases and efficient one-pot enzymatic synthesis of UDP-GlcA and UDP-GalA

Uridine 5′-diphosphate-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA), the unique carboxylic acid-formed sugar nucleotides, are key precursors involved in the biosynthesis of numerous cell components. Limited availability of those components has been hindering the development of efficient ways towards facile synthesis of bioactive glycans such as glycosaminoglycans. In current study, we biochemically characterized two UDP-sugar pyrophosphorylases from Arabidopsis thaliana (AtUSP) and Bifidobacterium infantis ATCC15697 (BiUSP), and compared their activities towards a panel of sugar-1-phosphates and derivatives. Both enzymes showed significant pyrophosphorylation activities towards GlcA-1-phosphate, and AtUSP also exhibited comparable activity towards GalA-1-phosphate. By combining with monosaccharide-1-phosphate kinases, we have developed an efficient and facile one-pot three-enzyme approach to quickly obtain hundreds milligrams of UDP-GlcA and UDP-GalA.

Improved one-pot multienzyme (OPME) systems for synthesizing UDP-uronic acids and glucuronides

Arabidopsis thaliana glucuronokinase (AtGlcAK) was cloned and shown to be able to use various uronic acids as substrates to produce the corresponding uronic acid-1-phosphates. AtGlcAK or Bifidobacterium infantis galactokinase (BiGalK) was used with a UDP-sugar pyrophosphorylase, an inorganic pyrophosphatase, with or without a glycosyltransferase for highly efficient synthesis of UDP-uronic acids and glucuronides. These improved cost-effective one-pot multienzyme (OPME) systems avoid the use of nicotinamide adenine dinucleotide (NAD+)-cofactor in dehydrogenase-dependent UDP-glucuronic acid production processes and can be broadly applied for synthesizing various glucuronic acid-containing molecules. This journal is

Biosynthesis of UDP-glucuronic acid and UDP-galacturonic acid in Bacillus cereus subsp. cytotoxis NVH 391-98

The food borne pathogen Bacillus cereus produces uronic acid-containing glycans that are secreted in a shielding biofilm environment, and certain alkaliphilic Bacillus deposit uronate-glycan polymers in the cell wall when adapting to alkaline environments. The source of these acidic sugars is unknown and, in the present study, we describe the functional identification of an operon in Bacillus cerues subsp. cytotoxis NVH 391-98 that comprises genes involved in the synthesis of UDP-uronic acids in Bacillus spp. Within the operon, a UDP-glucose 6-dehydrogenase converts UDP-glucose in the presence of NAD+ to UDP-glucuronic acid and NADH, and a UDP-GlcA 4-epimerase (UGlcAE) converts UDP-glucuronic acid to UDP-galacturonic acid. Interestingly, in vitro, both enzymes can utilize the TDP-sugar forms as well, albeit at lower catalytic efficiency. Unlike most of the very few bacterial 4-epimerases that have been characterized, which are promiscuous, the B. cereus UGlcAE enzyme is very specific and cannot use UDP-glucose, UDP-N-acetylglucosamine, UDP-N-acetylglucosaminuronic acid or UDP-xylose as substrates. Size exclusion chromatography suggests that UGlcAE is active as a monomer, unlike the dimeric form of plant enzymes; the Bacillus UDP-glucose 6-dehydrogenase is also found as a monomer. Phylogenic analysis further suggests that the Bacillus UGlcAE may have evolved separately from other bacterial and plant epimerases. Our results provide insight into the formation and function of uronic acid-containing glycans in the lifecycle of B. cereus and related species containing homologous operons, as well as a basis for determining the importance of these acidic glycans. We also discuss the ability to target UGlcAE as a drug candidate.