Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i>.

ABSTRACT: Prenylation increases the structural diversity and biological activity of flavonoids. In this study, an aromatic prenyltransferase, FgPT1, was identified from Fusarium globosum. This enzyme was demonstrated to specifically catalyze the prenylation of flavanones, including naringenin, hesperitin, eriodictyol, liquiritigenin, rac-pinocembrin, and dihydrogenistein, and exhibited no activity toward other types of flavonoids, including chalcones, flavonols, isoflavonoids, and flavonols. Ultra-performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS) and nuclear magnetic resonance (NMR) analysis indicated that the majority of prenylated products were 6-C prenyl flavanones, with the exception of liquiritigenin, which was additionally transformed to 4'-O prenyl l

SUBMITTER: Tang D 

PROVIDER: S-EPMC11990136 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature