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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Autores principales: Islam El-Awaad, Marco Bocola, Till Beuerle, Benye Liu, Ludger Beerhues
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea: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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