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Literature DB >> 25942062

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

Yuxi Guo¹, Junqiang Fang², Tiehai Li¹, Xu Li¹, Cheng Ma¹, Xuan Wang¹, Peng G Wang³, Lei Li⁴.

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.

Entities: CellLine Chemical Disease Gene Species

Keywords: Synthesis; UDP-GalA; UDP-GlcA; UDP-sugar pyrophosphorylase

Mesh：

Substances：

Year: 2015 PMID： 25942062 PMCID： PMC4481193 DOI： 10.1016/j.carres.2015.04.001

Source DB: PubMed Journal: Carbohydr Res ISSN： 0008-6215 Impact factor: 2.104

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