10345-04-7Relevant academic research and scientific papers
Improved one-pot multienzyme (OPME) systems for synthesizing UDP-uronic acids and glucuronides
Muthana, Musleh M.,Qu, Jingyao,Xue, Mengyang,Klyuchnik, Timofey,Siu, Alex,Li, Yanhong,Zhang, Lei,Yu, Hai,Li, Lei,Wang, Peng G.,Chen, Xi
supporting information, p. 4595 - 4598 (2015/05/27)
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
CHEMOENZYMATIC SYNTHESIS OF HEPARIN AND HEPARAN SULFATE ANALOGS
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Paragraph 0337; 0338; 0339; 0340, (2014/09/03)
The present invention provides a one-pot multi-enzyme method for preparing UDP-sugars from simple sugar starting materials. The invention also provides a one-pot multi-enzyme method for preparing oligosaccharides from simple sugar starting materials.
Cloning of glucuronokinase from Arabidopsis thaliana, the last missing enzyme of the myo-inositol oxygenase pathway to nucleotide sugars
Pieslinger, Anja Maria,Hoepflinger, Marion Christine,Tenhaken, Raimund
experimental part, p. 2902 - 2910 (2011/02/22)
Nucleotide sugars are building blocks for carbohydrate polymers in plant cell walls. They are synthesized from sugar-1-phosphates or epimerized as nucleotide sugars. The main precursor for primary cell walls is UDP-glucuronic acid, which can be synthesized via two independent pathways. One starts with the ring cleavage of myo-inositol into glucuronic acid, which requires a glucuronokinase and a pyrophosphorylase for activation into UDP-glucuronate. Here we report on the purification of glucuronokinase from Lilium pollen. A 40-kDa protein was purified combining six chromatographic steps and peptides were de novo sequenced. This allowed the cloning of the gene from Arabidopsis thaliana and the expression of the recombinant protein in Escherichia coli for biochemical characterization. Glucuronokinase is a novel member of the GHMP-kinase superfamily having an unique substrate specificity for D-glucuronic acid with a Km of 0.7 mM. It requires ATP as phosphate donor (K m 0.56mM). In Arabidopsis, the gene is expressed in all plant tissues with a preference for pollen. Genes for glucuronokinase are present in (all) plants, some algae, and a few bacteria as well as in some lower animals.
Process for selective oxidation of primary alcohols
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, (2008/06/13)
Primary alcohols, especially in carbohydrates, can be selectively oxidized to aldehydes and carboxylic acids in a low-halogen process by using a peracid in the presence of a catalytic amount of a di-tertiary-alkyl nitroxyl (TEMPO) and a catalytic amount of halide. The halide is preferably bromide and the process can be carried out at nearly neutral to moderately alkaline pH (5-11). The peracid can be produced or regenerated by means of hydrogen peroxide or oxygen. The process is advantageous for producing uronic acids and for introducing aldehyde groups which are suitable for crosslinking and derivatization.
