ArticlePloS one2018
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Functional characterization of BbCHI3 in regulating flavonoid biosynthesis and abiotic stress tolerance in Blumea balsamifera.BMC plant biology · 2026Article
- Biochemical evaluation of molecular parts for flavonoid production using plant synthetic biology.Frontiers in plant science · 2025Review
- Naringenin chalcone carbon double-bond reductases mediate dihydrochalcone biosynthesis in apple leaves.Plant physiology · 2024Article
- Structural and Interactional Analysis of the Flavonoid Pathway Proteins: Chalcone Synthase, Chalcone Isomerase and Chalcone Isomerase-like Protein.International journal of molecular sciences · 2024Article
- Biochemical and Molecular Characterization of the Rice Chalcone Isomerase Family.Plants (Basel, Switzerland) · 2021Article
- Adaptive Evolution of Chalcone Isomerase Superfamily in Fagaceae.Biochemical genetics · 2021Article
- Pluronic F-68 Improves Callus Proliferation of Recalcitrant Rice CultivarFrontiers in plant science · 2021Article
- Growth promoting effects of Pluronic F-68 on callus proliferation of recalcitrant rice cultivar.3 Biotech · 2020Article
- Identification and evolutionary analysis of chalcone isomerase-fold proteins in ferns.Journal of experimental botany · 2020Article
- Integrating molecular characterization and metabolites profile revealed CtCHI1's significant role in Carthamus tinctorius L.BMC plant biology · 2019Article
- iTRAQ Proteomic Analysis of Continuously Cropped Soybean Root Inoculated WithFrontiers in microbiology · 2019Article
- Chalcone Isomerase a Key Enzyme for Anthocyanin Biosynthesis inFrontiers in plant science · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chalcone isomerase (CHI) is an important enzyme for flavonoid biosynthesis that catalyzes the intramolecular cyclization of chalcones into (S)-flavanones. CHIs have been classified into two types based on their substrate specificity. Type I CHIs use naringenin chalcone as a substrate and are found in most of plants besides legumes, whereas type II CHIs in leguminous plants can also utilize isoliquiritigenin. In this study, we found that the CHI from the Antarctic plant Deschampsia antarctica (DaCHI1) is of type I based on sequence homology but can use type II CHI substrates. To clarify the enzymatic mechanism of DaCHI1 at the molecular level, the crystal structures of unliganded DaCHI1 and isoliquiritigenin-bound DaCHI1 were determined at 2.7 and 2.1 Å resolutions, respectively. The structures revealed that isoliquiritigenin binds to the active site of DaCHI1 and induces conformational changes. Additionally, the activity assay showed that while DaCHI1 exhibits substrate preference for naringenin chalcone, it can also utilize isoliquiritigenin although the catalytic activity was relatively low. Based on these results, we propose that DaCHI1 uses various substrates to produce antioxidant flavonoids as an adaptation to oxidative stresses associated with harsh environmental conditions.
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