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J Am Chem Soc. 2019 Apr 3. doi: 10.1021/jacs.8b10776. [Epub ahead of print]

An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments.

Author information

1
Molekulare Biotechnologie, Fachbereich Biowissenschaften, Goethe-Universität Frankfurt am Main and Buchmann Institute for Molecular Life Sciences (BMLS) , Goethe-Universität Frankfurt , Max-von-Laue-Straße 9 and 15 , 60438 Frankfurt am Main , Germany.
2
Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie , Technische Universität München , Lichtenbergstraße 4 , 85748 Garching , Germany.
3
Institut für Physikalische und Theoretische Chemie , Goethe-Universität Frankfurt , Max-von-Laue-Straße 7 , 60438 Frankfurt am Main , Germany.

Abstract

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 ApeI 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.

PMID:
30908039
DOI:
10.1021/jacs.8b10776

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