Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i>
Prenylation increases the structural diversity and biological activity of flavonoids. In this study, an aromatic prenyltransferase, FgPT1, was identified from <i>Fusarium globosum</i>. This enzyme was demonstrated to specifically catalyze the prenylation of flavanones, including naringen...
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| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-03-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/7/1558 |
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| Summary: | Prenylation increases the structural diversity and biological activity of flavonoids. In this study, an aromatic prenyltransferase, FgPT1, was identified from <i>Fusarium globosum</i>. 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-<i>C</i> prenyl flavanones, with the exception of liquiritigenin, which was additionally transformed to 4′-<i>O</i> prenyl liquiritigenin. Enzyme kinetic analysis suggested that FgPT1 exhibited the highest catalytic efficiency towards naringenin, with a <i>k<sub>cat</sub></i>/<i>K<sub>M</sub></i> value determined as 61.92 s<sup>−1</sup> M<sup>−1</sup>, and the lowest catalytic efficiency towards liquiritigenin, with a <i>k<sub>cat</sub></i>/<i>K<sub>M</sub></i> of 1.18 s<sup>−1</sup> M<sup>−1</sup>. Biochemical characterization suggested that FgPT1 functioned as a metal-dependent enzyme with optimal activity in the presence of Ba<sup>2+</sup> at pH 7.5 and 30 °C. Site-directed mutagenesis resulted in a series of mutants, including A325V with impaired prenylation activity and V116I, V181I, and V194I with enhanced activity. V194I displayed the highest enzymatic activity with a nine-fold increase compared to wild-type FgPT1. |
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| ISSN: | 1420-3049 |