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学科主题: 生命有机化学
题名: Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis
其他题名: FR901464生物合成中1个硫酯酶催化双键形成及酮酰合成酶催化转移
作者: He HY(贺海燕); Tang MC(唐满成); Zhang F(张凤); Tang GL(唐功利)
通讯作者: 唐功利
刊名: J. Am. Chem. Soc.
发表日期: 2014
DOI: 10.1021/ja500942y
卷: 136, 期:12, 页:4488-4491
收录类别: SCI
英文摘要: Modular polyketide synthases (PKSs) are well known to use ketosynthase (KS)-driven carbon-carbon bond formation, dehydratase-mediated dehydration to form double bonds, and product release by thioesterase (TE), all of which are regarded as the "canonical" roles for most polyketide biosyntheses. FR901464 is biosynthesized by a complex acyltransferase-less PKS system involving a nonterminal TE domain and several mutated KS domains. Here we demonstrate that this TE catalyzes the dehydration of the polyketide intermediate to yield a cis-double bond and a mutated KS transfers the nascent polyketide chain with only a cis-double bond to the downstream acyl carrier protein. These findings not only provide new insights into different enzymatic functions of PKS domains but also suggest an alternative strategy for cis-double bond formation during the polyketide assembly line.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/38939
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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作者单位: 中科院上海有机化学研究所

Recommended Citation:
He HY,Tang MC,Zhang F,et al. Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis[J]. J. Am. Chem. Soc.,2014,136(12):4488-4491.
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