Unusual substrate and halide versatility of phenolic halogenase PltM

Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural p...

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Autores principales: Mori, Shogo, Pang, Allan H., Thamban Chandrika, Nishad, Garneau-Tsodikova, Sylvie, Tsodikov, Oleg V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6424973/
https://www.ncbi.nlm.nih.gov/pubmed/30890712
http://dx.doi.org/10.1038/s41467-019-09215-9
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author Mori, Shogo
Pang, Allan H.
Thamban Chandrika, Nishad
Garneau-Tsodikova, Sylvie
Tsodikov, Oleg V.
author_facet Mori, Shogo
Pang, Allan H.
Thamban Chandrika, Nishad
Garneau-Tsodikova, Sylvie
Tsodikov, Oleg V.
author_sort Mori, Shogo
collection PubMed
description Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase.
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spelling pubmed-64249732019-03-21 Unusual substrate and halide versatility of phenolic halogenase PltM Mori, Shogo Pang, Allan H. Thamban Chandrika, Nishad Garneau-Tsodikova, Sylvie Tsodikov, Oleg V. Nat Commun Article Controlled halogenation of chemically versatile substrates is difficult to achieve. Here we describe a unique flavin-dependent halogenase, PltM, which is capable of utilizing a wide range of halides for installation on a diverse array of phenolic compounds, including FDA-approved drugs and natural products, such as terbutaline, fenoterol, resveratrol, and catechin. Crystal structures of PltM in complex with phloroglucinol and FAD in different states yield insight into substrate recognition and the FAD recycling mechanism of this halogenase. Nature Publishing Group UK 2019-03-19 /pmc/articles/PMC6424973/ /pubmed/30890712 http://dx.doi.org/10.1038/s41467-019-09215-9 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Mori, Shogo
Pang, Allan H.
Thamban Chandrika, Nishad
Garneau-Tsodikova, Sylvie
Tsodikov, Oleg V.
Unusual substrate and halide versatility of phenolic halogenase PltM
title Unusual substrate and halide versatility of phenolic halogenase PltM
title_full Unusual substrate and halide versatility of phenolic halogenase PltM
title_fullStr Unusual substrate and halide versatility of phenolic halogenase PltM
title_full_unstemmed Unusual substrate and halide versatility of phenolic halogenase PltM
title_short Unusual substrate and halide versatility of phenolic halogenase PltM
title_sort unusual substrate and halide versatility of phenolic halogenase pltm
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6424973/
https://www.ncbi.nlm.nih.gov/pubmed/30890712
http://dx.doi.org/10.1038/s41467-019-09215-9
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