Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis

Xanthones are pharmacologically and biosynthetically intriguing compounds. Here, the authors identify two cytochrome P450 enzymes, which hydroxylate and cyclize the benzophenone precursor to either 1,3,7- or 1,3,5-trihydroxyxanthones, and pinpoint residues that determine the alternative regioselecti...

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Auteurs principaux:	Islam El-Awaad, Marco Bocola, Till Beuerle, Benye Liu, Ludger Beerhues
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2016
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/24ea258c94a0425394112027bfe0fec6
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spelling	oai:doaj.org-article:24ea258c94a0425394112027bfe0fec62021-12-02T14:39:50ZBifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis10.1038/ncomms114722041-1723https://doaj.org/article/24ea258c94a0425394112027bfe0fec62016-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms11472https://doaj.org/toc/2041-1723Xanthones are pharmacologically and biosynthetically intriguing compounds. Here, the authors identify two cytochrome P450 enzymes, which hydroxylate and cyclize the benzophenone precursor to either 1,3,7- or 1,3,5-trihydroxyxanthones, and pinpoint residues that determine the alternative regioselectivities.Islam El-AwaadMarco BocolaTill BeuerleBenye LiuLudger BeerhuesNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Islam El-Awaad Marco Bocola Till Beuerle Benye Liu Ludger Beerhues Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
description	Xanthones are pharmacologically and biosynthetically intriguing compounds. Here, the authors identify two cytochrome P450 enzymes, which hydroxylate and cyclize the benzophenone precursor to either 1,3,7- or 1,3,5-trihydroxyxanthones, and pinpoint residues that determine the alternative regioselectivities.
format	article
author	Islam El-Awaad Marco Bocola Till Beuerle Benye Liu Ludger Beerhues
author_facet	Islam El-Awaad Marco Bocola Till Beuerle Benye Liu Ludger Beerhues
author_sort	Islam El-Awaad
title	Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
title_short	Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
title_full	Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
title_fullStr	Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
title_full_unstemmed	Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
title_sort	bifunctional cyp81aa proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/24ea258c94a0425394112027bfe0fec6
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Bifunctional CYP81AA proteins catalyse identical hydroxylations but alternative regioselective phenol couplings in plant xanthone biosynthesis

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