dc.identifier.uri |
http://dx.doi.org/10.15488/1036 |
|
dc.identifier.uri |
http://www.repo.uni-hannover.de/handle/123456789/1060 |
|
dc.contributor.author |
Williams, Katherine
|
|
dc.contributor.author |
Szwalbe, Agnieszka J.
|
|
dc.contributor.author |
Mulholland, Nicholas P.
|
|
dc.contributor.author |
Vincent, Jason L.
|
|
dc.contributor.author |
Bailey, Andrew M.
|
|
dc.contributor.author |
Willis, Christine L.
|
|
dc.contributor.author |
Simpson, Thomas J.
|
|
dc.contributor.author |
Cox, Russell J.
|
|
dc.date.accessioned |
2017-01-12T08:35:34Z |
|
dc.date.available |
2017-01-12T08:35:34Z |
|
dc.date.issued |
2016 |
|
dc.identifier.citation |
Williams, K.; Szwalbe, A.J.; Mulholland, N.P.; Vincent, J.L.; Bailey, A.M. et al.: Heterologous Production of Fungal Maleidrides Reveals the Cryptic Cyclization Involved in their Biosynthesis. In: Angewandte Chemie - International Edition 55 (2016), Nr. 23, S. 6784-6788. DOI: http://dx.doi.org/10.1002/anie.201511882 |
|
dc.description.abstract |
Fungal maleidrides are an important family of bioactive secondary metabolites that consist of 7, 8, or 9-membered carbocycles with one or two fused maleic anhydride moieties. The biosynthesis of byssochlamic acid (a nonadride) and agnestadride A (a heptadride) was investigated through gene disruption and heterologous expression experiments. The results reveal that the precursors for cyclization are formed by an iterative highly reducing fungal polyketide synthase supported by a hydrolase, together with two citrate-processing enzymes. The enigmatic ring formation is catalyzed by two proteins with homology to ketosteroid isomerases, and assisted by two proteins with homology to phosphatidylethanolamine-binding proteins. Ring cycle: The enzymes involved in the cyclization of the maleidride family of bioactive fungal natural products, including agnestadride A and byssochlamic acid, were identified. These previously unknown proteins show homology to ketosteroid isomerases (KI-like) and phosphatidylethanolamine-binding proteins (PEBP-like). |
eng |
dc.description.sponsorship |
BBSRC |
|
dc.description.sponsorship |
Syngenta |
|
dc.language.iso |
eng |
|
dc.publisher |
Weinheim : Wiley-VCH Verlag |
|
dc.relation.ispartofseries |
Angewandte Chemie - International Edition 55 (2016), Nr. 23 |
|
dc.rights |
CC BY 4.0 Unported |
|
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
|
dc.subject |
biosynthesis |
eng |
dc.subject |
cyclization |
eng |
dc.subject |
enzymes |
eng |
dc.subject |
maleidride |
eng |
dc.subject |
polyketides |
eng |
dc.subject |
Bins |
eng |
dc.subject |
Biochemistry |
eng |
dc.subject |
Biosynthesis |
eng |
dc.subject |
Enzymes |
eng |
dc.subject |
Fungi |
eng |
dc.subject |
Gene expression |
eng |
dc.subject |
Ketones |
eng |
dc.subject |
Metabolites |
eng |
dc.subject |
Proteins |
eng |
dc.subject |
Gene disruptions |
eng |
dc.subject |
Heterologous expression |
eng |
dc.subject |
Heterologous production |
eng |
dc.subject |
maleidride |
eng |
dc.subject |
Phosphatidylethanolamine |
eng |
dc.subject |
Polyketide synthases |
eng |
dc.subject |
Polyketides |
eng |
dc.subject |
Secondary metabolites |
eng |
dc.subject |
Cyclization |
eng |
dc.subject.ddc |
540 | Chemie
|
ger |
dc.title |
Heterologous Production of Fungal Maleidrides Reveals the Cryptic Cyclization Involved in their Biosynthesis |
|
dc.type |
Article |
|
dc.type |
Text |
|
dc.relation.issn |
1433-7851 |
|
dc.relation.doi |
https://doi.org/10.1002/anie.201511882 |
|
dc.bibliographicCitation.issue |
23 |
|
dc.bibliographicCitation.volume |
55 |
|
dc.bibliographicCitation.firstPage |
6784 |
|
dc.bibliographicCitation.lastPage |
6788 |
|
dc.description.version |
publishedVersion |
|
tib.accessRights |
frei zug�nglich |
|