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 |
|