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Updated: Jul 21, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Simultaneous one-pot multienzymatic synthesis and purification of Uridine-5'-Diphosphate-α-D-glucuronide and
Arnaud Pâris1, Tiffany Rundstadler1, Pierre Lafite1
1Institut de Chimie Organique et Analytique (ICOA), UMR 7311, CNRS-Université d'Orléans, Université d'Orléans, BP 6759, Orléans, 45067 Cedex 2, France.
Abstract:
Glucuronosyltransferases and xylosyltransferases are glycosyltransferases (GT) that are involved in a wide range of biological processes, including xenobiotic metabolism or proteoglycan biosynthesis and require as substrates activated sugar donors, respectively UDP-α-D-glucuronide (UDP-GlcA) and UDP-α-d-xylose (UDP-Xyl). As both nucleotide sugars are hardly available, we have developed a one-pot multienzymatic synthesis to produce sequentially UDP-GlcA and UDP-Xyl. This methodology involves the production of UDP-GlcA for glucuronic acid, coupling glucuronokinase and UDP-sugar pyrophosphorylase activities, followed by UDP-GlcA decarboxylation by UDP-Xylose Synthase. Each of these UDP-sugars can then be simultaneously purified and isolated from the unique reaction mixture, providing an efficient production methodology of these rare UDP-sugars for subsequent enzymatic studies of corresponding GT.
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