Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification

Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification

The biosynthesis of xiamycin, an antimicrobial bacterial indolosesquiterpenoid, involves an unusual cyclization cascade. Here, the authors characterise the XiaF enzyme, which resembles xenobiont-degrading enzymes and is responsible for a hidden indole hydroxylation step that triggers the cyclization...

Full description

Bibliographic Details
Main Authors: Susann Kugel, Martin Baunach, Philipp Baer, Mie Ishida-Ito, Srividhya Sundaram, Zhongli Xu, Michael Groll, Christian Hertweck
Format: Article
Language:English
Published: Nature Publishing Group 2017-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms15804
id doaj-423ff068b16c45a78cc7b351d616621f
record_format Article
spelling doaj-423ff068b16c45a78cc7b351d616621f2021-05-11T07:30:27ZengNature Publishing GroupNature Communications2041-17232017-06-018111310.1038/ncomms15804Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxificationSusann Kugel0Martin Baunach1Philipp Baer2Mie Ishida-Ito3Srividhya Sundaram4Zhongli Xu5Michael Groll6Christian Hertweck7Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)Department Chemie, Center for Integrated Protein Science Munich (CIPSM), Technische Universität MünchenDepartment of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)Department of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)Department Chemie, Center for Integrated Protein Science Munich (CIPSM), Technische Universität MünchenDepartment of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology (HKI)The biosynthesis of xiamycin, an antimicrobial bacterial indolosesquiterpenoid, involves an unusual cyclization cascade. Here, the authors characterise the XiaF enzyme, which resembles xenobiont-degrading enzymes and is responsible for a hidden indole hydroxylation step that triggers the cyclization reaction.https://doi.org/10.1038/ncomms15804
collection DOAJ
language English
format Article
sources DOAJ
author Susann Kugel
Martin Baunach
Philipp Baer
Mie Ishida-Ito
Srividhya Sundaram
Zhongli Xu
Michael Groll
Christian Hertweck
spellingShingle Susann Kugel
Martin Baunach
Philipp Baer
Mie Ishida-Ito
Srividhya Sundaram
Zhongli Xu
Michael Groll
Christian Hertweck
Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
Nature Communications
author_facet Susann Kugel
Martin Baunach
Philipp Baer
Mie Ishida-Ito
Srividhya Sundaram
Zhongli Xu
Michael Groll
Christian Hertweck
author_sort Susann Kugel
title Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
title_short Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
title_full Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
title_fullStr Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
title_full_unstemmed Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
title_sort cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-06-01
description The biosynthesis of xiamycin, an antimicrobial bacterial indolosesquiterpenoid, involves an unusual cyclization cascade. Here, the authors characterise the XiaF enzyme, which resembles xenobiont-degrading enzymes and is responsible for a hidden indole hydroxylation step that triggers the cyclization reaction.
url https://doi.org/10.1038/ncomms15804
work_keys_str_mv AT susannkugel crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT martinbaunach crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT philippbaer crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT mieishidaito crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT srividhyasundaram crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT zhonglixu crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT michaelgroll crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
AT christianhertweck crypticindolehydroxylationbyanoncanonicalterpenoidcyclaseparallelsbacterialxenobioticdetoxification
_version_ 1721452114884952064

Similar Items