Characterization of Heronamide Biosynthesis Reveals a Tailoring Hydroxylase and Indicates Migrated Double Bonds

Zhu Yiguang Zhang Wenjun Chen Yaolong Yuan Chengshan Zhang Haibo Zhang Guangtao Ma Liang Zhang Qingbo Tian Xin-Peng Zhang Si Zhang Changsheng · 2015

阅读量：101

生物合成

期刊名称：

ChemBioChem 2015 年 16 卷 14 期

发表日期：

2015.09.01

摘要：

Heronamides belong to a growing family of ??-amino acid polyketide macrolactams (??PMs) with an unsaturated side chain. The biosynthetic gene cluster for heronamide F was identified from the deep-sea-derived Streptomyces sp. SCSIO 03032. The involvement of the gene cluster in heronamide biosynthesis was confirmed by the functional characterization of the P450 enzyme HerO as an 8-hydroxylase for tailoring heronamide biosynthesis. The presence of migrated double bonds in the conjugated diene-containing side chain of heronamides was confirmed by feeding experiments with labeled small carboxylic acid molecules. This study is the first demonstration of migrated double bonds in ??PMs with an unsaturated side chain.