Structural highlights
Publication Abstract from PubMed
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 identi-fied all enzymes involved in APE biosynthesis and determined their peculiar functions. The biosynthesis was recon-stituted in vitro and ACP-bound intermediates were assigned for each reaction step by HPLC-MS. Native mass spec-trometry experiments identified four stable complexes: the acyl-carrier proteins ApeE and ApeF bound to the thi-oesterase ApeK, the dehydratases ApeI and ApeP as well as 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.
An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments.,Grammbitter GLC, Schmalhofer M, Karimi K, Schoner TA, Tobias NJ, Morgner N, Groll M, Bode HB J Am Chem Soc. 2019 Mar 25. doi: 10.1021/jacs.8b10776. PMID:30908039[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grammbitter GLC, Schmalhofer M, Karimi K, Schoner TA, Tobias NJ, Morgner N, Groll M, Bode HB. An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments. J Am Chem Soc. 2019 Mar 25. doi: 10.1021/jacs.8b10776. PMID:30908039 doi:http://dx.doi.org/10.1021/jacs.8b10776
