Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme

The polyketide synthase (PKS)‐like protein TerB, consisting of inactive dehydratase, inactive C‐methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6‐hydroxymellein, a key pathway intermediate during the biosynthesis of various fun...

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Autores principales: Kahlert, Lukas, Villanueva, Miranda, Cox, Russell J., Skellam, Elizabeth J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8251887/
https://www.ncbi.nlm.nih.gov/pubmed/33661567
http://dx.doi.org/10.1002/anie.202100969
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author Kahlert, Lukas
Villanueva, Miranda
Cox, Russell J.
Skellam, Elizabeth J.
author_facet Kahlert, Lukas
Villanueva, Miranda
Cox, Russell J.
Skellam, Elizabeth J.
author_sort Kahlert, Lukas
collection PubMed
description The polyketide synthase (PKS)‐like protein TerB, consisting of inactive dehydratase, inactive C‐methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6‐hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans‐interaction between iterative PKS components.
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spelling pubmed-82518872021-07-07 Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme Kahlert, Lukas Villanueva, Miranda Cox, Russell J. Skellam, Elizabeth J. Angew Chem Int Ed Engl Research Articles The polyketide synthase (PKS)‐like protein TerB, consisting of inactive dehydratase, inactive C‐methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6‐hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans‐interaction between iterative PKS components. John Wiley and Sons Inc. 2021-04-08 2021-05-10 /pmc/articles/PMC8251887/ /pubmed/33661567 http://dx.doi.org/10.1002/anie.202100969 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Research Articles
Kahlert, Lukas
Villanueva, Miranda
Cox, Russell J.
Skellam, Elizabeth J.
Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title_full Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title_fullStr Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title_full_unstemmed Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title_short Biosynthesis of 6‐Hydroxymellein Requires a Collaborating Polyketide Synthase‐like Enzyme
title_sort biosynthesis of 6‐hydroxymellein requires a collaborating polyketide synthase‐like enzyme
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8251887/
https://www.ncbi.nlm.nih.gov/pubmed/33661567
http://dx.doi.org/10.1002/anie.202100969
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