ArticleBMC plant biology2017
A new buckwheat dihydroflavonol 4-reductase (DFR), with a unique substrate binding structure, has altered substrate specificity.
Article in BMC plant biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 68 citations in OpenAlex.
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- Genotypic Variation of Purple Rice in Response to Shading in Yield, Anthocyanin Content, and Gene Expression.Plants (Basel, Switzerland) · 2023Article
- Development and chromosomal characterization of interspecific hybrids between common buckwheat (Breeding science · 2023Article
- Transcriptomic and Metabolomic Analyses Providing Insights into the Coloring Mechanism ofFoods (Basel, Switzerland) · 2022Article
- The complete chloroplast genome ofMitochondrial DNA. Part B, Resources · 2022Article
- Functional analysis of the dihydroflavonol 4-reductase family ofHorticulture research · 2022Article
- The Flavonoid Biosynthesis Network in Plants.International journal of molecular sciences · 2021Review
- Transcriptome Analysis Revealed the Mechanism by Which Exogenous ABA Increases Anthocyanins in Blueberry Fruit During Veraison.Frontiers in plant science · 2021Article
- Cloning and Functional Characterization of Dihydroflavonol 4-Reductase Gene Involved in Anthocyanin Biosynthesis of Chrysanthemum.International journal of molecular sciences · 2020Article
- Automatic Identification of Players in the Flavonoid Biosynthesis with Application on the Biomedicinal PlantPlants (Basel, Switzerland) · 2020Article
- Genetic and genomic research for the development of an efficient breeding system in heterostylous self-incompatible common buckwheat (Fagopyrum esculentum).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2020Review
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDihydroflavonol 4-reductase (DFR) is the key enzyme committed to anthocyanin and proanthocyanidin biosynthesis in the flavonoid biosynthetic pathway. DFR proteins can catalyse mainly the three substrates (dihydrokaempferol, dihydroquercetin, and dihydromyricetin), and show different substrate preferences. Although relationships between the substrate preference and amino acids in the region responsible for substrate specificity have been investigated in several plant species, the molecular basis of the substrate preference of DFR is not yet fully understood.
resultsBy using degenerate primers in a PCR, we isolated two cDNA clones that encoded DFR in buckwheat (Fagopyrum esculentum). Based on sequence similarity, one cDNA clone (FeDFR1a) was identical to the FeDFR in DNA databases (DDBJ/Gen Bank/EMBL). The other cDNA clone, FeDFR2, had a similar sequence to FeDFR1a, but a different exon-intron structure. Linkage analysis in an F
conclusionsWe isolated two buckwheat cDNA clones of DFR genes. FeDFR2 has unique structural and functional features that differ from those of previously reported DFRs in other plants. The 3D model suggested that not only the amino acid at the third position but also its neighbouring residues that are involved in the formation of the substrate-binding pocket play important roles in determining substrate preferences. The unique characteristics of FeDFR2 would provide a useful tool for future studies on the substrate specificity and organ-specific expression of DFRs.
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