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>Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase
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Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase
Prenylated xanthones are secondary metabolites with a broad spectrum of biological activities including antimicrobial and antitumor activities. One xanthone O -prenyltransferase XptB has been identified in Aspergillus nidulans . Recently, we characterised a bisindolyl benzoquinone C - and N -prenyltransferase AstPT from Aspergillus terreus with unusually high substrate specificity towards both the prenyl donor dimethylallyl diphosphate and acceptor bisindolyl benzoquinone. In this study, we demonstrate the acceptance of a number of hydroxyxanthones by AstPT in the presence of not only dimethylallyl but also geranyl and farnesyl diphosphate. Structural elucidation by HR-MS and NMR analyses proved the O -prenylation of all thirteen isolated enzyme products with different prenyl moieties. These results demonstrated the remarkable substrate and catalytic promiscuity of AstPT, which was recognised as a specific enzyme prior to this study.
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