ArticleCarbohydrate research2015
Comparing substrate specificity of two UDP-sugar pyrophosphorylases and efficient one-pot enzymatic synthesis of UDP-GlcA and UDP-GalA.
Article in Carbohydrate research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 29 citations in OpenAlex.
- Docking-guided rational engineering of a macrolide glycosyltransferase glycodiversifies epothilone B.Communications biology · 2022Article
- General Tolerance of Galactosyltransferases toward UDP-galactosamine Expands Their Synthetic Capability.Angewandte Chemie (International ed. in English) · 2021Article
- Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology.Food science and biotechnology · 2021Review
- Key Factors for A One-Pot Enzyme Cascade Synthesis of High Molecular Weight Hyaluronic Acid.International journal of molecular sciences · 2019Article
- Facile and Stereo-Selective Synthesis of UDP-α-D-xylose and UDP-β-L-arabinose Using UDP-Sugar Pyrophosphorylase.Frontiers in chemistry · 2018Article
- Chemoenzymatic Synthesis of a Library of Human Milk Oligosaccharides.The Journal of organic chemistry · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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Registered trials
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