Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.
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 i...
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ftdoajarticles:oai:doaj.org/article:dc1d8ef80dba414089d35a70e1b71dd6 2023-05-15T13:47:33+02:00 Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. Sun-Ha Park Chang Woo Lee Sung Mi Cho Hyoungseok Lee Hyun Park Jungeun Lee Jun Hyuck Lee 2018-01-01T00:00:00Z https://doi.org/10.1371/journal.pone.0192415 https://doaj.org/article/dc1d8ef80dba414089d35a70e1b71dd6 EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC5796730?pdf=render https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0192415 https://doaj.org/article/dc1d8ef80dba414089d35a70e1b71dd6 PLoS ONE, Vol 13, Iss 2, p e0192415 (2018) Medicine R Science Q article 2018 ftdoajarticles https://doi.org/10.1371/journal.pone.0192415 2022-12-31T14:52:35Z 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. Article in Journal/Newspaper Antarc* Antarctic Antarctica Directory of Open Access Journals: DOAJ Articles Antarctic The Antarctic PLOS ONE 13 2 e0192415 |
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Medicine R Science Q Sun-Ha Park Chang Woo Lee Sung Mi Cho Hyoungseok Lee Hyun Park Jungeun Lee Jun Hyuck Lee Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
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Medicine R Science Q |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Sun-Ha Park Chang Woo Lee Sung Mi Cho Hyoungseok Lee Hyun Park Jungeun Lee Jun Hyuck Lee |
author_facet |
Sun-Ha Park Chang Woo Lee Sung Mi Cho Hyoungseok Lee Hyun Park Jungeun Lee Jun Hyuck Lee |
author_sort |
Sun-Ha Park |
title |
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
title_short |
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
title_full |
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
title_fullStr |
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
title_full_unstemmed |
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv. |
title_sort |
crystal structure and enzymatic properties of chalcone isomerase from the antarctic vascular plant deschampsia antarctica desv. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2018 |
url |
https://doi.org/10.1371/journal.pone.0192415 https://doaj.org/article/dc1d8ef80dba414089d35a70e1b71dd6 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_source |
PLoS ONE, Vol 13, Iss 2, p e0192415 (2018) |
op_relation |
http://europepmc.org/articles/PMC5796730?pdf=render https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0192415 https://doaj.org/article/dc1d8ef80dba414089d35a70e1b71dd6 |
op_doi |
https://doi.org/10.1371/journal.pone.0192415 |
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PLOS ONE |
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13 |
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2 |
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e0192415 |
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1766247287258873856 |