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Cas Database

133-89-1

133-89-1

Identification

Synonyms:Uridine5'-(trihydrogen pyrophosphate), mono-a-D-glucopyranosyl ester (8CI);Uridine 5'-pyrophosphate,a-D-glucopyranosyl ester(6CI,7CI);UDP-D-glucose;UDP-Glc;UDP-Glucose;UDP-a-D-Glucose;UDPG;Uridine 5'-(trihydrogenpyrophosphate), mono-D-glucosyl ester;Uridine 5'-(a-D-glucopyranosyl pyrophosphate);Uridine5'-diphosphate glucose;Uridine 5'-diphospho-a-D-glucose;Uridine 5'-diphosphoglucose;Uridinediphosphate glucose;Uridine diphospho-D-glucose;Uridine diphosphoglucose;Uridine pyrophosphate-glucose;

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Safety information and MSDS view more

  • Signal Word:no data available

  • Hazard Statement:no data available

  • First-aid measures: General adviceConsult a physician. Show this safety data sheet to the doctor in attendance.If inhaled If breathed in, move person into fresh air. If not breathing, give artificial respiration. Consult a physician. In case of skin contact Wash off with soap and plenty of water. Consult a physician. In case of eye contact Rinse thoroughly with plenty of water for at least 15 minutes and consult a physician. If swallowed Never give anything by mouth to an unconscious person. Rinse mouth with water. Consult a physician.

  • Fire-fighting measures: Suitable extinguishing media Use water spray, alcohol-resistant foam, dry chemical or carbon dioxide. Wear self-contained breathing apparatus for firefighting if necessary.

  • Accidental release measures: Use personal protective equipment. Avoid dust formation. Avoid breathing vapours, mist or gas. Ensure adequate ventilation. Evacuate personnel to safe areas. Avoid breathing dust. For personal protection see section 8. Prevent further leakage or spillage if safe to do so. Do not let product enter drains. Discharge into the environment must be avoided. Pick up and arrange disposal. Sweep up and shovel. Keep in suitable, closed containers for disposal.

  • Handling and storage: Avoid contact with skin and eyes. Avoid formation of dust and aerosols. Avoid exposure - obtain special instructions before use.Provide appropriate exhaust ventilation at places where dust is formed. For precautions see section 2.2. Store in cool place. Keep container tightly closed in a dry and well-ventilated place.

  • Exposure controls/personal protection:Occupational Exposure limit valuesBiological limit values Handle in accordance with good industrial hygiene and safety practice. Wash hands before breaks and at the end of workday. Eye/face protection Safety glasses with side-shields conforming to EN166. Use equipment for eye protection tested and approved under appropriate government standards such as NIOSH (US) or EN 166(EU). Skin protection Wear impervious clothing. The type of protective equipment must be selected according to the concentration and amount of the dangerous substance at the specific workplace. Handle with gloves. Gloves must be inspected prior to use. Use proper glove removal technique(without touching glove's outer surface) to avoid skin contact with this product. Dispose of contaminated gloves after use in accordance with applicable laws and good laboratory practices. Wash and dry hands. The selected protective gloves have to satisfy the specifications of EU Directive 89/686/EEC and the standard EN 374 derived from it. Respiratory protection Wear dust mask when handling large quantities. Thermal hazards

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Relevant articles and documentsAll total 49 Articles be found

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Kalckar et al.

, p. 1038 (1953)

-

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Smith,Mills

, p. 152 (1955)

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Production of galactinol from sucrose by plant enzymes.

Wakiuchi, Nariaki,Shiomi, Ryohei,Tamaki, Hajime

, p. 1465 - 1471 (2003)

Galactinol, 1-O-(alpha-D-galactopyranosyl)-myo-inositol, was produced from sucrose as a starting material. UDP-Glc was prepared with sucrose and UDP using sucrose synthase partially purified from sweet potato roots. Then, the UDP-Glc was converted to UDP-Gal using yeast UDP-Gal 4-epimerase from a commercial source. Finally, galactinol was produced from the UDP-Gal and myo-inositol using galactinol synthase partially purified from cucumber leaves. The product was identified as galactinol by the retention times of HPLC, alpha-galactosidase digestion, and NMR spectrometry.

Transcriptome-wide identification of sucrose synthase genes in Ornithogalum caudatum

Li, Li-Na,Kong, Jian-Qiang

, p. 18778 - 18792 (2016)

OCAP-2-1, OCAP-2-2, OCAP-3-1 and OCAP-3-3, four glucose-containing polysaccharides from Ornithogalum caudatum, exhibit antitumor activity, suggesting their potential application as natural antitumor drugs. Although the incorporation of glucose into these polysaccharides from UDP-d-glucose is reasonably well understood, the cDNA isolation and functional characterization of genes responsible for UDP-d-glucose biosynthesis from O. caudatum has not been identified. Here, we present a full characterization of the sucrose synthase family, a Leloir glycosyltransferase responsible for UDP-d-glucose biosynthesis from O. caudatum. Specifically, a transcriptome-wide search for Sus genes in O. caudatum was first performed in the present study. A total of 5 unigenes sharing high sequence identity with Sus were retrieved from transcriptome sequencing. Three full-length Sus-like candidates derived from this unigene assembly were then obtained and isolated by reverse transcription polymerase chain reaction (RT-PCR) from O. caudatum. Additional analysis showed two conserved domains (sucrose synthase and glycosyl transferase domains) were present in this family. Phylogenetic analysis indicated that the OcSus1 and OcSus2 could be clustered together into a monocots specific clade, while OcSus3 could be classified into M & D1 category with members from the monocots and dicots species, displaying an evolutionary consistency with other plant species. These candidate isoenzymes were screened by functional expression in E. coli individually as standalone enzymes. All three cDNAs were identified to be bona fide genes and encoded sucrose synthase with varied kinetic properties. To further explore the possible role of these Sus proteins in polysaccharide biosynthesis, transcript profiles of the three genes were subsequently examined by real-time quantitative PCR in various tissues. OcSus1 and OcSus2 were therefore assumed to be responsible for the biosynthesis of the four glucose-containing polysaccharides due to their expression profiles in O. caudatum. Taken together, these data provide further comprehensive knowledge for polysaccharide biosynthesis in O. caudatum and broaden the potential application of Sus in metabolic engineering or synthetic biology as a potential gene part.

Efficient biosynthesis of uridine diphosphate glucose from maltodextrin by multiple enzymes immobilized on magnetic nanoparticles

Dong, Qing,Ouyang, Li-Ming,Yu, Hui-Lei,Xu, Jian-He

, p. 1622 - 1626 (2010)

Uridine diphosphate glucose (UDP-Glc) serves as a glucosyl donor in many enzymatic glycosylation processes. This paper describes a multiple enzyme, one-pot, biocatalytic system for the synthesis of UDP-Glc from low cost raw materials: maltodextrin and uridine triphosphate. Three enzymes needed for the synthesis of UDP-Glc (maltodextrin phosphorylase, glucose-1-phosphate thymidylytransferase, and pyrophosphatase) were expressed in Escherichia coli and then immobilized individually on amino-functionalized magnetic nanoparticles. The conditions for biocatalysis were optimized and the immobilized multiple-enzyme biocatalyst could be easily recovered and reused up to five times in repeated syntheses of UDP-Glc. After a simple purification, approximately 630 mg of crystallized UDP-Glc was obtained from 1 l of reaction mixture, for a moderate yield of around 50% (UTP conversion) at very low cost.

The uridyl transferase of liver.

MILLS,ONDARZA,SMITH

, p. 159 - 160 (1954)

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Enzyme Module Systems for the Synthesis of Uridine 5′-Diphospho-α- D -glucuronic Acid and Non-Sulfated Human Natural Killer Cell-1 (HNK-1) Epitope

Engels, Leonie,Henze, Manja,Hummel, Werner,Elling, Lothar

, p. 1751 - 1762 (2015)

Tailor-made strategies for the stereo- and regioselective multi-step enzymatic synthesis of glycoconjugates require well characterized glycosyltransferases and carbohydrate modifying enzymes. We here report on a novel enzyme cascade for the synthesis of uridine 5′-diphospho-α-D-glucuronic acid (UDP-GlcA) and the non-sulfated human natural killer cell-1 (HNK-1) epitope including in situ regeneration of UDP-GlcA and the cofactor nicotinamide adenine dinucleotide NAD+ by the combination of four enzymes in one-pot. In the first enzyme module sucrose synthase 1 (SuSy1) is used to produce uridine 5′-diphospho-α-D-glucose (UDP-Glc) from sucrose and uridine 5′-diphosphate (UDP). The combination with UDP-Glc dehydrogenase in the second enzyme module leads to the synthesis of UDP-GlcA with concomitant in situ regeneration of the cofactor NAD+ by nicotinamide adenine dinucleotide hydride (NADH)-oxidase. In the third enzyme module the mammalian glucuronyltransferase GlcAT-P catalyzes the synthesis of the non-sulfated HNK-1 epitope by regioselective transfer of GlcA onto N-acetyllactosamine type 2 (LacNAc type 2). We present a comprehensive study on substrate kinetics, substrate specificities, variation and relation of enzyme activities as well as cross inhibition of intermediate products. With optimized reaction conditions we obtain superior product yields with streamlined synthesis costs for the expensive nucleotide sugar UDP-GlcA and cofactor NAD+.

Enzyme formation in galactose-negative mutants of Escherichia coli

Kurahashi, Kiyoshi

, p. 114 - 116 (1957)

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Distribution of uridine diphosphate-glucose pyrophosphorylase in rat liver.

REID

, p. 251 - 253 (1959)

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A chemoenzymatic route to synthesize unnatural sugar nucleotides using a novel N-acetylglucosamine-1-phosphate pyrophosphorylase from Camphylobacter jejuni NCTC 11168

Fang, Junqiang,Xue, Mengyang,Gu, Guofeng,Liu, Xian-Wei,Wang, Peng George

, p. 4303 - 4307 (2013)

A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized.

Yeast uridine diphosphogalactose-4-epimerase, correlation between activity and fluorescence.

MAXWELL,DE ROBICHON-SZULMAJSTER,KALCKAR

, p. 407 - 415 (1958)

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Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12

Fang, Junqiang,Guan, Wanyi,Cai, Li,Gu, Guofeng,Liu, Xianwei,Wang, Peng George

, p. 6429 - 6432 (2009)

N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report th

-

Munch-Petersen et al.

, p. 1036 (1953)

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Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis

Yang, Ting,Echols, Merritt,Martin, Andy,Bar-Peled, Maor

, p. 275 - 284 (2010)

UDP-GlcNAc is an essential precursor for glycoprotein and glycolipid synthesis. In the present study, a functional nucleotidyltransferase gene from Arabidopsis encoding a 58.3 kDa GlcNAc1pUT-1 (N-acetylglucosamine-1-phosphate uridylyltransferase) was identified. In the forward reaction the enzyme catalyses the formation of UDP-N-acetylglucosamine and PPi from the respective monosaccharide 1-phosphate and UTP. The enzyme can utilize the 4-epimer UDP-GalNAc as a substrate as well. The enzyme requires divalent ions (Mg2+ or Mn2+) for activity and is highly active between pH 6.5 and 8.0, and at 30-37°C. The apparent Km values for the forward reaction were 337 μM (GlcNAc-1-P) and 295 μM (UTP) respectively. Another GlcNAc1pUT-2, which shares 86%amino acid sequence identity with GlcNAc1pUT-1, was found to convert, in addition to GlcNAc-1-P and GalNAc-1-P, Glc-1-P into corresponding UDP-sugars, suggesting that subtle changes in the UT family cause different substrate specificities. A three-dimensional protein structure model using the human AGX1 as template showed a conserved catalytic fold and helped identify key conserved motifs, despite the high sequence divergence. The identification of these strict and promiscuous gene products open a window to indentify new roles of amino sugar metabolism in plants and specifically their role as signalling molecules. The ability of GlcNAc1pUT-2 to utilize three different substrates may provide further understanding as to why biological systems have plasticity. The Authors.

Combined enzymatic synthesis of nucleotide (deoxy) sugars from sucrose and nucleoside monophosphates

Zervosen, Astrid,Stein, Andreas,Adrian, Holger,Elling, Lothar

, p. 2395 - 2404 (1996)

The synthesis of NDP-glucose 3a-d (N = A, C, U, dU) with sucrose synthase B was combined with the enzymatic synthesis of nucleoside diphosphates 2a-d from their corresponding nucleoside monophosphates 1a-d by different kinases A. Further combination with

Large scale enzymatic synthesis of oligosaccharides and a novel purification process

Zhou, Guangyan,Liu, Xianwei,Su, Doris,Li, Lei,Xiao, Min,Wang, Peng G.

, p. 311 - 314 (2011)

Herein we report the practical chemo enzymatic synthesis of trisaccharide and derivatives of iGb3 and Gb3, and a novel purification process using immobilized yeast to remove the monosaccharide from the reaction mixture. High purity oligosaccharide compoun

-

Kurahashi,Anderson

, p. 498 (1958)

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Catalytic reversibility of Pyrococcus horikoshii trehalose synthase: Efficient synthesis of several nucleoside diphosphate glucoses with enzyme recycling

Ryu, Soo-In,Kim, Jeong-Eun,Kim, Eun-Joo,Chung, Seung-Kyung,Lee, Soo-Bok

, p. 128 - 134 (2011)

The trehalose synthase (TreT) from Pyrococcus horikoshii represented reversible catalysis in alternative synthesis of trehalose and nucleoside 5′-diphosphate-glucose (NDP-Glc), depending on the substrates involved. TreT from P. horikoshii had differential preferences on NDP-Glc as a donor for trehalose synthesis, in which guanosine 5′-diphosphate (GDP)-Glc was the most favored in terms of reaction specificity, kcat/Km. Uridine 5′-diphosphate (UDP)- and adenosine 5′-diphosphate (ADP)-Glcs were employed with less preferences. This enzyme reversely cleaved trehalose to transfer the glucosyl moiety to various NDPs, efficiently producing NDP-Glcs. Although ADP-Glc was the least favorable donor, the counterpart, ADP, was the most favorable acceptor for the reverse synthesis of NDP-Glc in k cat/Km. GDP and UDP were less preferred, compared to ADP. In a batch reaction of 12 h, the molar yield of NDP-Glc per NDP used was decreased approximately in the order of ADP-Glc > GDP-Glc > cytidine 5′-diphosphate (CDP)-Glc or UDP-Glc. The overall productivity of the enzyme was largely improved in a gram scale for NDP-Glcs using repetitive batch reactions with enzyme recycling. Thus, it is suggested that TreT from P. horikoshii may be useful for the regeneration of NDP-Glc from NDP, especially for ADP-Glc from ADP, with trehalose as a glucose resource.

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

Zou, Yang,Xue, Mengyang,Wang, Wenjun,Cai, Li,Chen, Leilei,Liu, Jun,Wang, Peng George,Shen, Jie,Chen, Min

, p. 76 - 81 (2013)

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.

One-Step Synthesis of Sugar Nucleotides

Miyagawa, Atsushi,Toyama, Sanami,Ohmura, Ippei,Miyazaki, Shun,Kamiya, Takeru,Yamamura, Hatsuo

, p. 15645 - 15651 (2020)

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.

Glycosyltransferase Co-Immobilization for Natural Product Glycosylation: Cascade Biosynthesis of the C-Glucoside Nothofagin with Efficient Reuse of Enzymes

Liu, Hui,Tegl, Gregor,Nidetzky, Bernd

supporting information, p. 2157 - 2169 (2021/03/08)

Sugar nucleotide-dependent (Leloir) glycosyltransferases are synthetically important for oligosaccharides and small molecule glycosides. Their practical use involves one-pot cascade reactions to regenerate the sugar nucleotide substrate. Glycosyltransferase co-immobilization is vital to advance multi-enzyme glycosylation systems on solid support. Here, we show glycosyltransferase chimeras with the cationic binding module Zbasic2 for efficient and well-controllable two-enzyme co-immobilization on anionic (ReliSorb SP400) carrier material. We use the C-glycosyltransferase from rice (Oryza sativa; OsCGT) and the sucrose synthase from soybean (Glycine max; GmSuSy) to synthesize nothofagin, the natural 3’-C-β-d-glucoside of the dihydrochalcone phloretin, with regeneration of uridine 5’-diphosphate (UDP) glucose from sucrose and UDP. Exploiting enzyme surface tethering via Zbasic2, we achieve programmable loading of the glycosyltransferases (~18 mg/g carrier; 60%–70% yield; ~80% effectiveness) in an activity ratio (OsCGT:GmSuSy=~1.2) optimal for the overall reaction rate (~0.2 mmol h?1 g?1 catalyst; 30 °C, pH 7.5). Using phloretin solubilized at 120 mM as inclusion complex with 2-hydroxypropyl-β-cyclodextrin, we demonstrate complete substrate conversion into nothofagin (~52 g/L; 21.8 mg product h?1 g?1 catalyst) at 4% mass loading of the catalyst. The UDP-glucose was recycled 240 times. The solid catalyst showed excellent reusability, retaining ~40% of initial activity after 15 cycles of phloretin conversion (60 mM) with a catalyst turnover number of ~273 g nothofagin/g protein used. Our study presents important progress towards applied bio-catalysis with immobilized glycosyltransferase cascades. (Figure presented.).

Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from: Streptococcus pneumonia serotype 23F

Chen, Zonggang,Gu, Guofeng,Jin, Guoxia,Li, Siqiang,Wang, Hong

, p. 30110 - 30114 (2020/09/07)

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.

Enzymatic Synthesis of Human Milk Fucosides α1,2-Fucosyl para-Lacto-N-Hexaose and its Isomeric Derivatives

Fang, Jia-Lin,Tsai, Teng-Wei,Liang, Chin-Yu,Li, Jyun-Yi,Yu, Ching-Ching

supporting information, p. 3213 - 3219 (2018/08/06)

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.).

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

Eixelsberger, Thomas,Horvat, Doroteja,Gutmann, Alexander,Weber, Hansj?rg,Nidetzky, Bernd

supporting information, p. 2503 - 2507 (2017/02/23)

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.

Process route upstream and downstream products

Process route

α-D-Glucopyranoside 1-(disodium phosphate)
56401-20-8

α-D-Glucopyranoside 1-(disodium phosphate)

uridine 5'-triphosphate sodium salt
19817-92-6

uridine 5'-triphosphate sodium salt

UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With inorganic pyrophosphatase; uridine-5'-diphosphoglucose pyrophosphorylase; enzymatically at pH 7.6;
Conditions
Conditions Yield
With phosphoglucomutase; inorganic pyrophosphatase; PAN-immobilized UDP-Glc pyrophosphorylase; In water; for 20h; pH 7.5;
6 mmol
disodium uridine-5'-monophosphate
3387-36-8

disodium uridine-5'-monophosphate

Sucrose
57-50-1

Sucrose

UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With bovine serum albumine; phospho(enol)pyruvate CHA-salt; tris hydrochloride; uridine 5'-triphosphate trisodium salt; magnesium chloride; diothiothreitol; at 30 ℃; for 21h; sucrose synthase, pyruvate kinase, nucleoside monophosphate kinase;
21%
(2R,3S,4S,5R,6S)-2-Hydroxymethyl-6-(3-methoxy-pyridin-2-yloxy)-tetrahydro-pyran-3,4,5-triol

(2R,3S,4S,5R,6S)-2-Hydroxymethyl-6-(3-methoxy-pyridin-2-yloxy)-tetrahydro-pyran-3,4,5-triol

UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
In N,N-dimethyl-formamide; for 190h; Yield given; Yields of byproduct given. Title compound not separated from byproducts; Ambient temperature;
In N,N-dimethyl-formamide; for 3.16667h; Yield given; Yields of byproduct given. Title compound not separated from byproducts; Ambient temperature;
UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
dicyclohexyl-carbodiimide
538-75-0

dicyclohexyl-carbodiimide

UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With N,N-dimethyl-formamide; acetonitrile;
UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With pyridine;
UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With tributyl-amine; benzene; Hydrogenation.an Palladium/Kohle in wss. Aethanol;
UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
With tributyl-amine; benzene; Hydrogenation.an Palladium/Kohle in wss. Aethanol;
UDP-glucose
133-89-1

UDP-glucose

Conditions
Conditions Yield
reversible enzymatische Bildung mit Hilfe von UDPglucose-4-epimerase aus Hefe;
reversible enzymatische Bildung mit Hilfe von UDPglucose-4-epimerase aus Leberextrakten;

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