Oxidative steps during the biosynthesis of squalestatin S1

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dc.identifier.uri http://dx.doi.org/10.15488/5195
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/5242
dc.contributor.author Lebe, Karen E.
dc.contributor.author Cox, Russell J.
dc.date.accessioned 2019-08-15T11:13:37Z
dc.date.available 2019-08-15T11:13:37Z
dc.date.issued 2018
dc.identifier.citation Lebe, Karen E.; Cox, Russell J.: Oxidative steps during the biosynthesis of squalestatin S1. In: Chemical Science 10 (2018), Nr. 4, S. 1227-1231. DOI: https://doi.org/10.1039/c8sc02615g
dc.description.abstract The squalestatins are a class of highly complex fungal metabolites which are potent inhibitors of squalene synthase with potential use in the control of cholesterol biosynthesis. Little is known of the chemical steps involved in the construction of the 4,8-dioxa-bicyclo[3.2.1]octane core. Here, using a combination of directed gene knockout and heterologous expression experiments, we show that two putative non-heme-iron-dependent enzymes appear to catalyse a remarkable series of six consecutive oxidations which set up the bioactive core of the squalestatins. This is followed by the action of an unusual copper-dependent oxygenase which introduces a hydroxyl required for later acetylation. eng
dc.language.iso eng
dc.publisher Cambridge : Royal Society of Chemistry
dc.relation.ispartofseries Chemical Science 10 (2018), Nr. 4
dc.rights CC BY-NC 3.0
dc.rights.uri https://creativecommons.org/licenses/by-nc/3.0/
dc.subject Heterologous expression eng
dc.subject ATP synthase eng
dc.subject Acetylation eng
dc.subject Oxygenase eng
dc.subject Organic chemistry eng
dc.subject Enzyme eng
dc.subject Chemistry eng
dc.subject Squalene eng
dc.subject Biosynthesis eng
dc.subject Biochemistry eng
dc.subject Gene knockout eng
dc.subject.ddc 540 | Chemie ger
dc.title Oxidative steps during the biosynthesis of squalestatin S1
dc.type article
dc.type Text
dc.relation.issn 2041-6520
dc.relation.doi https://doi.org/10.1039/c8sc02615g
dc.bibliographicCitation.issue 4
dc.bibliographicCitation.volume 10
dc.bibliographicCitation.firstPage 1227
dc.bibliographicCitation.lastPage 1231
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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