ArticlePlanta2020
Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis.
Article in Planta, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 34 citations in OpenAlex.
- Two shikimate dehydrogenases play an essential role in the biosynthesis of galloylated catechins in tea plants.Horticulture research · 2025Article
- Chemodiversity, biosynthetic regulation, and functional roles ofFrontiers in plant science · 2025Review
- Elucidation and reconstitution of hydrolyzable tannin biosynthesis.Plant biotechnology (Tokyo, Japan) · 2024Article
- Genome-wide identification of TCP transcription factors and their potential roles in hydrolyzable tannin production inFrontiers in plant science · 2024Article
- Biosynthetic pathway of prescription bergenin fromFrontiers in plant science · 2023Article
- Molecular Cloning, Expression, and Functional Analysis of Glycosyltransferase (TbUGGT) Gene fromMolecules (Basel, Switzerland) · 2022Article
- The Eucalyptus grandis chloroplast proteome: Seasonal variations in leaf development.PloS one · 2022Article
- Identification and Characterization of Glucosyltransferase That Forms 1-Galloyl-Molecules (Basel, Switzerland) · 2021Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
MAIN
conclusionEucalyptus camaldulensis EcDQD/SDH2 and 3 combine gallate formation, dehydroquinate dehydratase, and shikimate dehydrogenase activities. They are candidates for providing the essential gallate for the biosynthesis of the aluminum-detoxifying metabolite oenothein B. The tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of E. camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. In our approach to elucidate the biosynthesis of oenothein B, we here report on the identification of E. camaldulensis enzymes that catalyze the formation of gallate, which is the phenolic constituent of hydrolyzable tannins. By systematical screening of E. camaldulensis dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs), we found two enzymes, EcDQD/SDH2 and 3, catalyzing the NADP
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