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Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase

[Image: see text] By mining fungal genomic information, a noncanonical iterative type I PKS fused with an N-terminal adenylation–thiolation didomain, which catalyzes the formation of naringenin chalcone, was found. Structural prediction and molecular docking analysis indicated that a C-terminal thio...

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Autores principales: Furumura, Sho, Ozaki, Taro, Sugawara, Akihiro, Morishita, Yohei, Tsukada, Kento, Ikuta, Tatsuya, Inoue, Asuka, Asai, Teigo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society and American Society of Pharmacognosy 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9972472/
https://www.ncbi.nlm.nih.gov/pubmed/36762727
http://dx.doi.org/10.1021/acs.jnatprod.2c01027
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author Furumura, Sho
Ozaki, Taro
Sugawara, Akihiro
Morishita, Yohei
Tsukada, Kento
Ikuta, Tatsuya
Inoue, Asuka
Asai, Teigo
author_facet Furumura, Sho
Ozaki, Taro
Sugawara, Akihiro
Morishita, Yohei
Tsukada, Kento
Ikuta, Tatsuya
Inoue, Asuka
Asai, Teigo
author_sort Furumura, Sho
collection PubMed
description [Image: see text] By mining fungal genomic information, a noncanonical iterative type I PKS fused with an N-terminal adenylation–thiolation didomain, which catalyzes the formation of naringenin chalcone, was found. Structural prediction and molecular docking analysis indicated that a C-terminal thioesterase domain was involved in the Claisen-type cyclization. An enzyme responsible for formation of (2S)-flavanone in the biosynthesis of fungal flavonoids was also identified. Collectively, these findings demonstrate unprecedented fungal biosynthetic machinery leading to plant-like metabolites.
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spelling pubmed-99724722023-03-01 Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase Furumura, Sho Ozaki, Taro Sugawara, Akihiro Morishita, Yohei Tsukada, Kento Ikuta, Tatsuya Inoue, Asuka Asai, Teigo J Nat Prod [Image: see text] By mining fungal genomic information, a noncanonical iterative type I PKS fused with an N-terminal adenylation–thiolation didomain, which catalyzes the formation of naringenin chalcone, was found. Structural prediction and molecular docking analysis indicated that a C-terminal thioesterase domain was involved in the Claisen-type cyclization. An enzyme responsible for formation of (2S)-flavanone in the biosynthesis of fungal flavonoids was also identified. Collectively, these findings demonstrate unprecedented fungal biosynthetic machinery leading to plant-like metabolites. American Chemical Society and American Society of Pharmacognosy 2023-02-10 /pmc/articles/PMC9972472/ /pubmed/36762727 http://dx.doi.org/10.1021/acs.jnatprod.2c01027 Text en © 2023 The Authors. Published by American Chemical Society and American Society of Pharmacognosy https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Furumura, Sho
Ozaki, Taro
Sugawara, Akihiro
Morishita, Yohei
Tsukada, Kento
Ikuta, Tatsuya
Inoue, Asuka
Asai, Teigo
Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title_full Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title_fullStr Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title_full_unstemmed Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title_short Identification and Functional Characterization of Fungal Chalcone Synthase and Chalcone Isomerase
title_sort identification and functional characterization of fungal chalcone synthase and chalcone isomerase
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9972472/
https://www.ncbi.nlm.nih.gov/pubmed/36762727
http://dx.doi.org/10.1021/acs.jnatprod.2c01027
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