Heterologous Production of Fungal Maleidrides Reveals the Cryptic Cyclization Involved in their Biosynthesis

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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
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 Text
dc.type article
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

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