Highly Promiscuous Flavonoid Di-O-glycosyltransferases from Carthamus tinctorius L

Safflower (Carthamus tinctorius L.) has been recognized for its medicinal value, but there have been limited studies on the glycosyltransferases involved in the biosynthesis of flavonoid glycosides from safflower. In this research, we identified two highly efficient flavonoid O-glycosyltransferases, CtOGT1 and CtOGT2, from safflower performing local BLAST alignment. By constructing a prokaryotic expression vector, we conducted in vitro enzymatic reactions and discovered that these enzymes were capable of catalyzing two-step O-glycosylation using substrates such as kaempferol, quercetin, and eriodictyol. Moreover, they exhibited efficient catalytic activity towards various compounds, including flavones (apigenin, scutellarein), dihydrochalcone (phloretin), isoflavones (genistein, daidzein), flavanones (naringenin, glycyrrhizin), and flavanonols (dihydrokaempferol), leading to the formation of O-glycosides. The broad substrate specificity of these enzymes is noteworthy. This study provides valuable insights into the biosynthetic pathways of flavonoid glycosides in safflower. The discovery of CtOGT1 and CtOGT2 enhances our understanding of the enzymatic processes involved in synthesizing flavonoid glycosides in safflower, contributing to the overall comprehension of secondary metabolite biosynthesis in this plant species.

Medienart:

E-Artikel

Erscheinungsjahr:

2024

Erschienen:

2024

Enthalten in:

Zur Gesamtaufnahme - volume:29

Enthalten in:

Molecules (Basel, Switzerland) - 29(2024), 3 vom: 26. Jan.

Sprache:

Englisch

Beteiligte Personen:

Xu, Xiaoyu [VerfasserIn]
Xia, Meng [VerfasserIn]
Han, Yang [VerfasserIn]
Tan, Honghu [VerfasserIn]
Chen, Yanying [VerfasserIn]
Song, Xinqi [VerfasserIn]
Yuan, Shijun [VerfasserIn]
Zhang, Yifeng [VerfasserIn]
Su, Ping [VerfasserIn]
Huang, Luqi [VerfasserIn]

Links:

Volltext

Themen:

Carthamus tinctorius L.
Di-O-glycosyltransferases
EC 2.4.-
Flavones
Flavonoid glycosides
Flavonoids
Glycosides
Glycosyltransferases
Journal Article

Anmerkungen:

Date Completed 14.02.2024

Date Revised 14.02.2024

published: Electronic

Citation Status MEDLINE

doi:

10.3390/molecules29030604

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM368278379