Modular Oxime Formation by a trans-AT Polyketide Synthase.

Bacterial Natural Products Biosynthesis Oxime Polyketides X-Ray Crystallography

Journal

Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543

Informations de publication

Date de publication:
21 08 2023
Historique:
received: 29 03 2023
medline: 18 8 2023
pubmed: 22 5 2023
entrez: 22 5 2023
Statut: ppublish

Résumé

Modular trans-acyltransferase polyketide synthases (trans-AT PKSs) are enzymatic assembly lines that biosynthesize complex polyketide natural products. Relative to their better studied cis-AT counterparts, the trans-AT PKSs introduce remarkable chemical diversity into their polyketide products. A notable example is the lobatamide A PKS, which incorporates a methylated oxime. Here we demonstrate biochemically that this functionality is installed on-line by an unusual oxygenase-containing bimodule. Furthermore, analysis of the oxygenase crystal structure coupled with site-directed mutagenesis allows us to propose a model for catalysis, as well as identifying key protein-protein interactions that support this chemistry. Overall, our work adds oxime-forming machinery to the biomolecular toolbox available for trans-AT PKS engineering, opening the way to introducing such masked aldehyde functionalities into diverse polyketides.

Identifiants

pubmed: 37216334
doi: 10.1002/anie.202304481
doi:

Substances chimiques

Polyketide Synthases 79956-01-7
Polyketides 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202304481

Informations de copyright

© 2023 Wiley-VCH Verlag GmbH.

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Auteurs

Hannah A Minas (HA)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

Romain M M François (RMM)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.
Université de Lorraine, CNRS, IMoPA, 54000, Nancy, France.

Franziska Hemmerling (F)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

Amy E Fraley (AE)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

Cora L Dieterich (CL)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

Simon H Rüdisser (SH)

Institute of Molecular Biology and Biophysics, Biomolecular NMR Spectroscopy Platform, Eidgenössische Technische Hochschule (ETH) Zürich, Hönggerbergring 64, 8093, Zürich, Switzerland.

Roy A Meoded (RA)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

Sabrina Collin (S)

Université de Lorraine, CNRS, IMoPA, 54000, Nancy, France.

Kira J Weissman (KJ)

Université de Lorraine, CNRS, IMoPA, 54000, Nancy, France.

Arnaud Gruez (A)

Université de Lorraine, CNRS, IMoPA, 54000, Nancy, France.

Jörn Piel (J)

Institute of Microbiology, Eidgenössische Technische Hochschule (ETH) Zürich, Vladimir-Prelog-Weg 4, 8093, Zürich, Switzerland.

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