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Journal Article

An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments


Karimi,  Kudratullah
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;


Groll,  Michael
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Grammbitter, G. L. C., Schmalhofer, M., Karimi, K., Shi, Y.-M., Schoener, T. A., Tobias, N. J., et al. (2019). An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 141(42), 16615-16623. doi:10.1021/jacs.8b10776.

Cite as: https://hdl.handle.net/21.11116/0000-000A-0564-0
Aryl polyene (APE) pigments are a widely distributed class of bacterial polyketides. So far, little is known about the biosynthesis of these compounds, which are produced by a novel type II polyketide synthase (PKS). We have identified all enzymes involved in APE biosynthesis and determined their peculiar functions. The biosynthesis was reconstituted in vitro, and ACP-bound intermediates were assigned for each reaction step by HPLC-MS. Native mass spectrometry experiments identified four stable complexes: the acyl-carrier proteins ApeE and ApeF bound to the thioesterase ApeK, the dehydratases Apel and ApeP, and the ketosynthase ApeO in complex with its chain-length factor ApeC. X-ray structures of the heterodimeric ApeO:ApeC and ApeI:ApeP complexes depict striking protein-protein interactions. Altogether, our study elucidated mechanistic aspects of APE biosynthesis that unifies elements of type II fatty acid and PKS systems, but in addition includes novel enzyme complexes.