dc.identifier.uri |
http://dx.doi.org/10.15488/110 |
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dc.identifier.uri |
http://www.repo.uni-hannover.de/handle/123456789/128 |
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dc.contributor.author |
Kandziora, Nadine
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dc.contributor.author |
Andexer, Jennifer N.
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dc.contributor.author |
Moss, Steven J.
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dc.contributor.author |
Wilkinson, Barrie
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dc.contributor.author |
Leadlay, Peter F.
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dc.contributor.author |
Hahn, Frank
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dc.date.accessioned |
2015-11-19T12:59:55Z |
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dc.date.available |
2015-11-19T12:59:55Z |
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dc.date.issued |
2014-06-30 |
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dc.identifier.citation |
Kandziora, Nadine; Andexer, Jennifer N.; Moss, Steven J.; Wilkinson, Barrie; Leadlay, Peter F.; Hahn, Frank: Uncovering the origin of Z-configured double bonds in polyketides: intermediate E-double bond formation during borrelidin biosynthesis. In: Chemical Science 5 (2014), Nr. 9, S. 3563-3567. DOI: http://dx.doi.org/10.1039/c4sc00883a |
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dc.description.abstract |
Formation of Z-configured double bonds in reduced polyketides is uncommon and their origins have not been extensively studied. To investigate the origin of the Z-configured double bond in the macrolide borrelidin, the recombinant dehydratase domains BorDH2 and B0rDH3 were assayed with a synthetic analogue of the predicted tetraketide substrate. The configuration of the dehydrated products was determined to be E in both cases by comparison to synthetic standards. Detailed NMR spectroscopic analysis of the biosynthetic intermediate pre-borrelidin confirmed the E,E-configuration of the fulllength polyketide synthase product. In contrast to a previously-proposed hypothesis, our results show that in this case the Z-configured double bond is not formed via dehydration from a 3 L-configured precursor, but rather as the result of a later isomerization process. |
eng |
dc.description.sponsorship |
Marie Curie programme of the European Union |
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dc.description.sponsorship |
Emmy Noether programme of the Deutsche Forschungsgemeinschaft |
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dc.description.sponsorship |
DAAD |
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dc.language.iso |
eng |
eng |
dc.publisher |
Cambridge : Royal Society of Chemistry |
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dc.relation.ispartofseries |
Chemical Science 5 (2014), Nr. 9 |
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dc.rights |
Es gilt deutsches Urheberrecht. Das Dokument darf zum eigenen Gebrauch kostenfrei genutzt, aber nicht im Internet bereitgestellt oder an Außenstehende weitergegeben werden. Dieser Beitrag ist aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich. |
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dc.subject |
Angiogenesis Inhibitor Borrelidin |
eng |
dc.subject |
Synthase Ketoreductase Domain |
eng |
dc.subject |
Streptomyces-Parvulus TU4055 |
eng |
dc.subject |
Dehydratase Domain |
eng |
dc.subject |
Gene-Cluster |
eng |
dc.subject |
In-Vitro |
eng |
dc.subject |
Stereospecificity |
eng |
dc.subject |
Crystal |
eng |
dc.subject |
Stereochemistry |
eng |
dc.subject |
(-)-borrelidin |
eng |
dc.subject |
Borrelidin |
eng |
dc.subject.ddc |
540 | Chemie
|
ger |
dc.title |
Uncovering the origin of Z-configured double bonds in polyketides: intermediate E-double bond formation during borrelidin biosynthesis |
eng |
dc.type |
Article |
|
dc.type |
Text |
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dc.relation.essn |
2041-6539 |
|
dc.relation.issn |
2041-6520 |
|
dc.relation.doi |
http://dx.doi.org/10.1039/c4sc00883a |
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dc.bibliographicCitation.issue |
9 |
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dc.bibliographicCitation.volume |
5 |
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dc.bibliographicCitation.firstPage |
3563 |
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dc.bibliographicCitation.lastPage |
3567 |
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dc.description.version |
publishedVersion |
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tib.accessRights |
frei zug�nglich |
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