Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols

Monooxygenases exhibiting high activity and differing regioselectivity for the dietary isoflavone metabolite equol were discovered among enzymes in the HpaBC family by a genome mining approach. These enzymes enabled the one-step product-selective synthesis of 3′- and 6-hydroxyequols from equol and m...

Descripción completa

Detalles Bibliográficos
Autores principales: Hashimoto, Takafumi, Nozawa, Daiki, Mukai, Katsuyuki, Matsuyama, Akinobu, Kuramochi, Kouji, Furuya, Toshiki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9066559/
https://www.ncbi.nlm.nih.gov/pubmed/35518870
http://dx.doi.org/10.1039/c9ra03913a
_version_ 1784699819120394240
author Hashimoto, Takafumi
Nozawa, Daiki
Mukai, Katsuyuki
Matsuyama, Akinobu
Kuramochi, Kouji
Furuya, Toshiki
author_facet Hashimoto, Takafumi
Nozawa, Daiki
Mukai, Katsuyuki
Matsuyama, Akinobu
Kuramochi, Kouji
Furuya, Toshiki
author_sort Hashimoto, Takafumi
collection PubMed
description Monooxygenases exhibiting high activity and differing regioselectivity for the dietary isoflavone metabolite equol were discovered among enzymes in the HpaBC family by a genome mining approach. These enzymes enabled the one-step product-selective synthesis of 3′- and 6-hydroxyequols from equol and molecular oxygen.
format Online
Article
Text
id pubmed-9066559
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher The Royal Society of Chemistry
record_format MEDLINE/PubMed
spelling pubmed-90665592022-05-04 Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols Hashimoto, Takafumi Nozawa, Daiki Mukai, Katsuyuki Matsuyama, Akinobu Kuramochi, Kouji Furuya, Toshiki RSC Adv Chemistry Monooxygenases exhibiting high activity and differing regioselectivity for the dietary isoflavone metabolite equol were discovered among enzymes in the HpaBC family by a genome mining approach. These enzymes enabled the one-step product-selective synthesis of 3′- and 6-hydroxyequols from equol and molecular oxygen. The Royal Society of Chemistry 2019-07-15 /pmc/articles/PMC9066559/ /pubmed/35518870 http://dx.doi.org/10.1039/c9ra03913a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Hashimoto, Takafumi
Nozawa, Daiki
Mukai, Katsuyuki
Matsuyama, Akinobu
Kuramochi, Kouji
Furuya, Toshiki
Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title_full Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title_fullStr Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title_full_unstemmed Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title_short Monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
title_sort monooxygenase-catalyzed regioselective hydroxylation for the synthesis of hydroxyequols
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9066559/
https://www.ncbi.nlm.nih.gov/pubmed/35518870
http://dx.doi.org/10.1039/c9ra03913a
work_keys_str_mv AT hashimototakafumi monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols
AT nozawadaiki monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols
AT mukaikatsuyuki monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols
AT matsuyamaakinobu monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols
AT kuramochikouji monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols
AT furuyatoshiki monooxygenasecatalyzedregioselectivehydroxylationforthesynthesisofhydroxyequols

Ejemplares similares