| Literature DB >> 16984884 |
Tiangang Liu1, Delin You, Chiara Valenzano, Yuhui Sun, Jialiang Li, Qing Yu, Xiufen Zhou, David E Cane, Zixin Deng.
Abstract
The polyketide synthase (PKS) for the biosynthesis of the polyether nanchangmycin lacks an apparent thioesterase comparable to the type I thioesterase domains of the modular PKSs responsible for macrolide biosynthesis. Three candidate polyether chain-releasing factors were examined. Both the putative CR domain and the NanE protein appeared to be genetically relevant. Among the three heterologously expressed soluble proteins (recombinant CR domain, the ACP-CR didomain, and NanE) tested, only NanE hydrolyzed the polyether-SNAC. By contrast, recombinant DEBS TE from the erythromycin pathway, and the recombinant MonAX, a type II TE associated with the polyether monensin biosynthesis for which a homolog has not been detected in the nanchangmycin cluster, hydrolyzed a diketide-SNAC but not the polyether-SNAC. We could thus conclude that NanE is a dedicated thioesterase mediating the specific release of the polyether chain during nanchangmycin biosynthesis.Entities:
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Year: 2006 PMID： 16984884 DOI： 10.1016/j.chembiol.2006.07.006
Source DB: PubMed Journal: Chem Biol ISSN： 1074-5521