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...
Saved in:
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-03-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/7/1558 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850212757132017664 |
|---|---|
| author | Dingtao Tang Jiajie Quan Zhengjiao Gao Bingfeng He Yu Hou Peipei Fan Meidong Pan Jiali Yang |
| author_facet | Dingtao Tang Jiajie Quan Zhengjiao Gao Bingfeng He Yu Hou Peipei Fan Meidong Pan Jiali Yang |
| author_sort | Dingtao Tang |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-07cd2c85188f4ebd92a054b0e7be25e1 |
| institution | OA Journals |
| issn | 1420-3049 |
| language | English |
| publishDate | 2025-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj-art-07cd2c85188f4ebd92a054b0e7be25e12025-08-20T02:09:17ZengMDPI AGMolecules1420-30492025-03-01307155810.3390/molecules30071558Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i>Dingtao Tang0Jiajie Quan1Zhengjiao Gao2Bingfeng He3Yu Hou4Peipei Fan5Meidong Pan6Jiali Yang7School of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaPrenylation 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.https://www.mdpi.com/1420-3049/30/7/1558enzyme catalysisflavanonesubstrate specificitysite-directed mutagenesis |
| spellingShingle | Dingtao Tang Jiajie Quan Zhengjiao Gao Bingfeng He Yu Hou Peipei Fan Meidong Pan Jiali Yang Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> Molecules enzyme catalysis flavanone substrate specificity site-directed mutagenesis |
| title | Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> |
| title_full | Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> |
| title_fullStr | Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> |
| title_full_unstemmed | Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> |
| title_short | Prenylation of Flavanones by an Aromatic Prenyltransferase from <i>Fusarium globosum</i> |
| title_sort | prenylation of flavanones by an aromatic prenyltransferase from i fusarium globosum i |
| topic | enzyme catalysis flavanone substrate specificity site-directed mutagenesis |
| url | https://www.mdpi.com/1420-3049/30/7/1558 |
| work_keys_str_mv | AT dingtaotang prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT jiajiequan prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT zhengjiaogao prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT bingfenghe prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT yuhou prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT peipeifan prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT meidongpan prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi AT jialiyang prenylationofflavanonesbyanaromaticprenyltransferasefromifusariumglobosumi |