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Due to their broad substrate scope, DMATSs are anticipated as biotechnological tools for producing bioactive prenylated aromatic compounds. Our study explored the substrate scope and product profile of a recombinant RePT, a novel DMATS from the thermophilic fungus <jats:italic>Rasamsonia emersonii.<\/jats:italic> Among a variety of aromatic substrates, RePT showed the highest substrate conversion for <jats:sc>l<\/jats:sc>-tryptophan and <jats:sc>l<\/jats:sc>-tyrosine (&gt;\u200990%), yielding two mono-prenylated products in both cases. Nine phenolics from diverse phenolic subclasses were notably converted (&gt;\u200910%), of which the stilbenes oxyresveratrol, piceatannol, pinostilbene, and resveratrol were the best acceptors (37\u201355% conversion). The position of prenylation was determined using NMR spectroscopy or annotated using MS<jats:sup>2<\/jats:sup> fragmentation patterns, demonstrating that RePT mainly catalyzed mono-<jats:italic>O<\/jats:italic>-prenylation on the hydroxylated aromatic substrates. On <jats:sc>l<\/jats:sc>-tryptophan, a non-hydroxylated substrate, it preferentially catalyzed <jats:italic>C<\/jats:italic>7 prenylation with reverse <jats:italic>N<\/jats:italic>1 prenylation as a secondary reaction. Moreover, RePT also possessed substrate-dependent organic solvent tolerance in the presence of 20% (<jats:italic>v\/v<\/jats:italic>) methanol or DMSO, where a significant conversion (&gt;\u200990%) was maintained. Our study demonstrates the potential of RePT as a biocatalyst for the production of bioactive prenylated aromatic amino acids, stilbenes, and various phenolic compounds.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Key points<\/jats:title>\n            <jats:p>\u2022 <jats:italic>RePT catalyzes prenylation of diverse aromatic substrates.<\/jats:italic>\n            <\/jats:p>\n            <jats:p>\u2022 <jats:italic>RePT enables O-prenylation of phenolics, especially stilbenes.<\/jats:italic>\n            <\/jats:p>\n            <jats:p>\u2022 <jats:italic>The novel RePT remains active in 20% methanol or DMSO.<\/jats:italic>\n            <\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Graphical abstract<\/jats:title>\n          <\/jats:sec>","DOI":"10.1007\/s00253-024-13254-8","type":"journal-article","created":{"date-parts":[[2024,7,18]],"date-time":"2024-07-18T08:01:51Z","timestamp":1721289711000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Prenylation of aromatic amino acids and plant phenolics by an aromatic prenyltransferase from Rasamsonia emersonii"],"prefix":"10.1007","volume":"108","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7432-5359","authenticated-orcid":false,"given":"Pimvisuth","family":"Chunkrua","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-3539-6213","authenticated-orcid":false,"given":"Kai P.","family":"Leschonski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9979-0927","authenticated-orcid":false,"given":"Alejandro A.","family":"Gran\u2010Scheuch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8088-500X","authenticated-orcid":false,"given":"Gijs J. 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