Uridine diphosphate glucosyl transferase

Biosynthesis R. is derived from vomilenine, an intermediate in the biosynthetic pathway to the antiarrhyth-mic ajmaline, by glucosylation. The corresponding glucosyl transferase is membrane-bound, dependent on uridine diphosphate glucose, and has a high substrate specificity. A soluble, substrate-specific glu-cosidase effects the reversal of this reaction see also Rauvolfia alkaloids. 

Uridine diphosphate glucose (UDP-Glc) serves as a glucosyl donor in many enzymatic glycosylation processes. A multiple enzyme, one-pot, biocatalytic system was developed 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-l-phosphate thymidyly-transferase, 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, with a moderate yield of around 50% (UTP conversion) at very low cost. ... 

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