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• W2078353492 abstract "Prenylated indole alkaloids derived from L-tryptophan are widely distributed in nature and show diverse biological and pharmacological activities, usually distinct from their non-prenylated precursors. Prenyltransferases catalyze the transfer reactions of prenyl moieties onto the indole nucleus and contribute largely to the structural diversity of these compounds. In this study, we demonstrate the acceptance of cyclo-L-homotryptophan-D-valine, an unnatural cyclic dipeptide, by eight prenyltransferases of the dimethylallyltryptophan synthase superfamily. Seven products with one prenyl moiety at each position of the indole nucleus and one diprenylated derivative were isolated from enzyme assays of cyclo-L-homotryptophan-D-valine with dimethylallyl diphosphate. To the best of our knowledge, this is the first report for production of seven monoprenylated products from one substrate by one-step reactions." @default.
• W2078353492 created "2016-06-24" @default.
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• W2078353492 date "2013-09-09" @default.
• W2078353492 modified "2023-09-30" @default.
• W2078353492 title "One Substrate - Seven Products with Different Prenylation Positions in One-Step Reactions: Prenyltransferases Make it Possible" @default.
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• W2078353492 doi "https://doi.org/10.1002/adsc.201300386" @default.
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