133-89-1Relevant articles and documents
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Kalckar et al.
, p. 1038 (1953)
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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.
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.
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+.
Distribution of uridine diphosphate-glucose pyrophosphorylase in rat liver.
REID
, p. 251 - 253 (1959)
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Yeast uridine diphosphogalactose-4-epimerase, correlation between activity and fluorescence.
MAXWELL,DE ROBICHON-SZULMAJSTER,KALCKAR
, p. 407 - 415 (1958)
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Munch-Petersen et al.
, p. 1036 (1953)
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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
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Kurahashi,Anderson
, p. 498 (1958)
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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.
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.).
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.).
