Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides

Rubromycin family of natural products belongs to aromatic polyketides with diverse bioactivities, but details of their biosynthesis are limited. Here, the authors report the complete in vitro reconstitution of enzymatic formation of the spiroketal moiety of rubromycin polyketides, driven by flavin-d...

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Autores principales:	Britta Frensch, Thorsten Lechtenberg, Michel Kather, Zeynep Yunt, Martin Betschart, Bernd Kammerer, Steffen Lüdeke, Michael Müller, Jörn Piel, Robin Teufel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2c66fdf660624127ac29372efbed73b9
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spelling	oai:doaj.org-article:2c66fdf660624127ac29372efbed73b92021-12-02T13:14:47ZEnzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides10.1038/s41467-021-21432-92041-1723https://doaj.org/article/2c66fdf660624127ac29372efbed73b92021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21432-9https://doaj.org/toc/2041-1723Rubromycin family of natural products belongs to aromatic polyketides with diverse bioactivities, but details of their biosynthesis are limited. Here, the authors report the complete in vitro reconstitution of enzymatic formation of the spiroketal moiety of rubromycin polyketides, driven by flavin-dependent enzymes, and characterize reaction intermediates.Britta FrenschThorsten LechtenbergMichel KatherZeynep YuntMartin BetschartBernd KammererSteffen LüdekeMichael MüllerJörn PielRobin TeufelNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Britta Frensch Thorsten Lechtenberg Michel Kather Zeynep Yunt Martin Betschart Bernd Kammerer Steffen Lüdeke Michael Müller Jörn Piel Robin Teufel Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
description	Rubromycin family of natural products belongs to aromatic polyketides with diverse bioactivities, but details of their biosynthesis are limited. Here, the authors report the complete in vitro reconstitution of enzymatic formation of the spiroketal moiety of rubromycin polyketides, driven by flavin-dependent enzymes, and characterize reaction intermediates.
format	article
author	Britta Frensch Thorsten Lechtenberg Michel Kather Zeynep Yunt Martin Betschart Bernd Kammerer Steffen Lüdeke Michael Müller Jörn Piel Robin Teufel
author_facet	Britta Frensch Thorsten Lechtenberg Michel Kather Zeynep Yunt Martin Betschart Bernd Kammerer Steffen Lüdeke Michael Müller Jörn Piel Robin Teufel
author_sort	Britta Frensch
title	Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
title_short	Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
title_full	Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
title_fullStr	Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
title_full_unstemmed	Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
title_sort	enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/2c66fdf660624127ac29372efbed73b9
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Enzymatic spiroketal formation via oxidative rearrangement of pentangular polyketides

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