Characterization of Heronamide Biosynthesis Reveals a Tailoring Hydroxylase and Indicates Migrated Double Bonds
Characterization of Heronamide Biosynthesis Reveals a Tailoring Hydroxylase and Indicates Migrated Double Bonds
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DOI：
10.1002/cbic.201500281
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发表时间：
2015-09-21
期刊：
影响因子：
3.2
通讯作者：
Zhang, Changsheng
中科院分区：
文献类型：
--
作者：
Zhu, Yiguang;Zhang, Wenjun;Zhang, Changsheng
Heronamides属于具有不饱和侧链的β-氨基酸聚酮大环内酰胺（β PM）的不断增长的家族。从深海来源的链霉菌SCSIO 03032中鉴定出heronamide F的生物合成基因簇。通过P450酶HerO作为用于定制Heronamide生物合成的8-羟化酶的功能表征证实了基因簇参与Heronamide生物合成。通过用标记的小羧酸分子进行饲喂实验，证实了在heronamides的含共轭二烯侧链中存在迁移的双键。这项研究是第一次证明迁移的双键在β PM与不饱和侧链。
Heronamides belong to a growing family of beta-amino acid polyketide macrolactams (beta 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 beta PMs with an unsaturated side chain.