An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments

Gina L.C. Grammbitter, Maximilian Schmalhofer, Kudratullah Karimi, Yi Ming Shi, Tim A. Schöner, Nicholas J. Tobias, Nina Morgner, Michael Groll, Helge B. Bode

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

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.

Original languageEnglish
Pages (from-to)16615-16623
Number of pages9
JournalJournal of the American Chemical Society
Volume141
Issue number42
DOIs
StatePublished - 23 Oct 2019

Fingerprint

Dive into the research topics of 'An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments'. Together they form a unique fingerprint.

Cite this