Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme

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dc.identifier.uri http://dx.doi.org/10.15488/14957
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/15076
dc.contributor.author Kahlert, Lukas
dc.contributor.author Villanueva, Miranda
dc.contributor.author Cox, Russell J.
dc.contributor.author Skellam, Elizabeth J.
dc.date.accessioned 2023-10-16T07:34:26Z
dc.date.available 2023-10-16T07:34:26Z
dc.date.issued 2021
dc.identifier.citation Kahlert, L.; Villanueva, M.; Cox, R.J.; Skellam, E.J.: Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme. In: Angewandte Chemie International Edition 60 (2021), Nr. 20, S. 11423-11429. DOI: https://doi.org/10.1002/anie.202100969
dc.description.abstract The polyketide synthase (PKS)-like protein TerB, consisting of inactive dehydratase, inactive C-methyltransferase, and functional ketoreductase domains collaborates with the iterative non reducing PKS TerA to produce 6-hydroxymellein, a key pathway intermediate during the biosynthesis of various fungal natural products. The catalytically inactive dehydratase domain of TerB appears to mediate productive interactions with TerA, demonstrating a new mode of trans-interaction between iterative PKS components. eng
dc.language.iso eng
dc.publisher Weinheim : Wiley-VCH
dc.relation.ispartofseries Angewandte Chemie International Edition 60 (2021), Nr. 20
dc.rights CC BY-NC 4.0 Unported
dc.rights.uri https://creativecommons.org/licenses/by-nc/4.0
dc.subject iterative polyketide synthase eng
dc.subject ketoreductase eng
dc.subject mellein eng
dc.subject terrein eng
dc.subject trans-acting domain eng
dc.subject.ddc 540 | Chemie
dc.title Biosynthesis of 6-Hydroxymellein Requires a Collaborating Polyketide Synthase-like Enzyme eng
dc.type Article
dc.type Text
dc.relation.essn 1521-3773
dc.relation.issn 1433-7851
dc.relation.doi https://doi.org/10.1002/anie.202100969
dc.bibliographicCitation.issue 20
dc.bibliographicCitation.volume 60
dc.bibliographicCitation.firstPage 11423
dc.bibliographicCitation.lastPage 11429
dc.description.version publishedVersion eng
tib.accessRights frei zug�nglich


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