ArticleFrontiers in plant science2016
Molecular Cloning and Functional Characterization of a Novel (Iso)flavone 4',7-O-diglucoside Glucosyltransferase from Pueraria lobata.
Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 39 citations in OpenAlex.
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- Genome-wide analysis of UDP-glycosyltransferase gene family and identification of a flavonoid 7-O-UGT (AhUGT75A) enhancing abiotic stress in peanut (Arachis hypogaea L.).BMC plant biology · 2023Article
- A Muti-Substrate FlavonolMolecules (Basel, Switzerland) · 2023Article
- Glycosylation and methylation in the biosynthesis of isoflavonoids inFrontiers in plant science · 2023Review
- Comparative analysis of the medicinal and nutritional components of different varieties ofFrontiers in plant science · 2023Article
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- Evaluation of pathways to thePlant direct · 2022Article
- Chloroplast genomes of two Pueraria DC. species: sequencing, comparative analysis and molecular marker development.FEBS open bio · 2022Article
- Functional Characterization of a Novel Glycosyltransferase (UGT73CD1) from Iris tectorum Maxim. for the Substrate promiscuity.Molecular biotechnology · 2021Article
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- Transcriptome sequencing and analysis reveals the molecular response to selenium stimuli inPeerJ · 2020Article
- Comprehensive transcriptome analysis reveals genes potentially involved in isoflavone biosynthesis in Pueraria thomsonii Benth.PloS one · 2019Article
- Identification of Three (Iso)flavonoid Glucosyltransferases FromFrontiers in plant science · 2019Article
- Global Transcriptome Analyses Reveal Differentially Expressed Genes of Six Organs and Putative Genes Involved in (Iso)flavonoid Biosynthesis inFrontiers in plant science · 2018Article
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Pueraria lobata roots accumulate a rich source of isoflavonoid glycosides, including 7-O- and 4'-O-mono-glucosides, and 4',7-O-diglucosides, which have numerous human health benefits. Although, isoflavonoid 7-O-glucosyltranferases (7-O-UGTs) have been well-characterized at molecular levels in legume plants, genes, or enzymes that are required for isoflavonoid 4'-O- and 4',7-O-glucosylation have not been identified in P. lobata to date. Especially for the 4',7-O-di-glucosylations, the genetic control for this tailing process has never been elucidated from any plant species. Through transcriptome mining, we describe here the identification and characterization of a novel UGT (designated PlUGT2) governing the isoflavonoid 4',7-O-di-glucosylations in P. lobata. Biochemical roles of PlUGT2 were assessed by in vitro assays with PlUGT2 protein produced in Escherichia coli and analyzed for its qualitative substrate specificity. PlUGT2 was active with various (iso)flavonoid acceptors, catalyzing consecutive glucosylation activities at their O-4' and O-7 positions. PlUGT2 was most active with genistein, a general isoflavone in legume plants. Real-time PCR analysis showed that PlUGT2 is preferentially transcribed in roots relative to other organs of P. lobata, which is coincident with the accumulation pattern of 4'-O-glucosides and 4',7-O-diglucosides in P. lobata. The identification of PlUGT2 would help to decipher the P. lobata isoflavonoid glucosylations in vivo and may provide a useful enzyme catalyst for an efficient biotransformation of isoflavones or other natural products for food or pharmacological purposes.
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