ArticleCommunications biology2022
The protein conformational basis of isoflavone biosynthesis.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Discovery of an isoflavone biosynthetic pathway in Iridaceae plants.Nature communications · 2026Article
- An assessment of the cytochrome P450 2-hydroxyisoflavanone synthase (2-HIS) crystal structure.Communications biology · 2026Article
- Reply to: an assessment of the cytochrome P450 2-hydroxyisoflavanone synthase (2-HIS) crystal structure.Communications biology · 2026Article
- Key genes in a "Galloylation-Degalloylation cycle" controlling the synthesis of hydrolyzable tannins in strawberry plants.Horticulture research · 2025Article
- Advances in synthesizing plant-derived isoflavones and their precursors with multiple pharmacological activities using engineered yeasts.Microbial cell factories · 2025Review
- Recent advances in understanding the regulation of plant secondary metabolite biosynthesis by ethylene-mediated pathways.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Systematic Engineering ofJournal of fungi (Basel, Switzerland) · 2024Article
- Article
- Evolution and diversification of carboxylesterase-like [4+2] cyclases in aspidosperma and iboga alkaloid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biosynthesis and metabolic engineering of isoflavonoids in model plants and crops: a review.Frontiers in plant science · 2024Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. Their biosynthesis is initiated by two enzymes with unusual catalytic activities; 2-hydroxyisoflavanone synthase (2-HIS), a membrane-bound cytochrome P450 catalyzing a coupled aryl-ring migration and hydroxylation, and 2-hydroxyisoflavanone dehydratase (2-HID), a member of a large carboxylesterase family that paradoxically catalyzes dehydration of 2-hydroxyisoflavanones to isoflavone. Here we report the crystal structures of 2-HIS from Medicago truncatula and 2-HID from Pueraria lobata. The 2-HIS structure reveals a unique cytochrome P450 conformation and heme and substrate binding mode that facilitate the coupled aryl-ring migration and hydroxylation reactions. The 2-HID structure reveals the active site architecture and putative catalytic residues for the dual dehydratase and carboxylesterase activities. Mutagenesis studies revealed key residues involved in substrate binding and specificity. Understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.