Abstract
Plants produce various prenylated phenolic metabolites, including flavonoids, phloroglucinols, and coumarins, many of which have multiple prenyl moieties and display various biological activities. Prenylated phenylpropanes, such as artepillin C (3,5-diprenyl-p-coumaric acid), exhibit a broad range of pharmaceutical effects. To date, however, no prenyltransferases (PTs) involved in the biosynthesis of phenylpropanes and no plant enzymes that introduce multiple prenyl residues to native substrates with different regio-specificities have been identified. This study describes the isolation from Artemisia capillaris of a phenylpropane-specific PT gene, AcPT1, belonging to UbiA superfamily. This gene encodes a membrane-bound enzyme, which accepts p-coumaric acid as its specific substrate and transfers two prenyl residues stepwise to yield artepillin C. These findings provide novel insights into the molecular evolution of this gene family, contributing to the chemical diversification of plant specialized metabolites. These results also enabled the design of a yeast platform for the synthetic biology of artepillin C.
Highlights
Plants produce various prenylated phenolic metabolites, including flavonoids, phloroglucinols, and coumarins, many of which have multiple prenyl moieties and display various biological activities
A. capillaris was selected as the source of the gene encoding phenylpropanespecific PT for two major reasons: (1) the Brazilian plant B. dracunculifolia, which accumulates large quantities of artepillin C, is not available in Japan, and (2) A. capillaris is an Asteraceaeous plant that produces capillartemisin A and B, which are hydroxylated derivatives of artepillin C30, along with artepillin C, suggesting that PTs for phenylpropanoids are highly expressed
We searched for NCBI nucleotide collection for Asteraceae polypeptide sequences in all six UbiA subfamilies involved in plant primary metabolism, i.e., homogentisate phytyltransferase for tocopherol, homogentisate solanesyltransferase (VTE2-2) for plastoquinone, 1,4-dihydroxy-2-naphthoic acid phytyltransferase for phylloquinone, chlorophyll synthase (ATG4), protoheme IX farnesyltransferase for Heam a, and phydroxybenzoate polyprenyltransferase (PPT) for ubiquinone (Fig. 1)[17]
Summary
Plants produce various prenylated phenolic metabolites, including flavonoids, phloroglucinols, and coumarins, many of which have multiple prenyl moieties and display various biological activities. This study describes the isolation from Artemisia capillaris of a phenylpropanespecific PT gene, AcPT1, belonging to UbiA superfamily This gene encodes a membranebound enzyme, which accepts p-coumaric acid as its specific substrate and transfers two prenyl residues stepwise to yield artepillin C. Brazilian green propolis is one of the most globally widespread types used for commercial purposes and is characterized by the presence of bioactive prenylated derivatives of pcoumaric acid, such as drupanin and artepillin C, as major constituents, with concentrations frequently exceeding 10%6–9 These ingredients were exploited as collation markers to identify the botanical origin of the propolis as leaves of an Asteraceae bush, Baccharis dracunculifolia[7]. Assessments of multiple prenylated phenolic compounds have not well understood whether different PTs are responsible for individual prenylations, or whether one enzyme catalyzes the multiple prenylation reactions
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
