Characterization of the Ketosynthase and Acyl Carrier Protein Domains at the LnmI Nonribosomal Peptide Synthetase-Polyketide Synthase Interface for Leinamycin Biosynthesis

Yong Huang, Gong Li Tang, Guohui Pan, Chin-Yuan Chang, Ben Shen*

*此作品的通信作者

研究成果: Article同行評審

10 引文 斯高帕斯(Scopus)

摘要

Leinamycin (LNM) is biosynthesized by a hybrid nonribosomal peptide synthetase (NRPS)-acyltransferase (AT)-less type I polyketide synthase (PKS). Characterization of LnmI revealed ketosynthase (KS)-acyl carrier protein (ACP)-KS domains at the NRPS-PKS interface. Inactivation of the KS domain or ACP domain in vivo abolished LNM production, and the ACP domain can be phosphopantetheinylated in vitro. The LnmI KS-ACP-KS architecture represents a new mechanism for functional crosstalk between NRPS and AT-less type I PKS in the biosynthesis of hybrid peptide-polyketide natural products.

原文English
頁(從 - 到)4288-4291
頁數4
期刊Organic Letters
18
發行號17
DOIs
出版狀態Published - 2 9月 2016

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