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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
He HY(贺海燕); Tang MC(唐满成); Zhang F(张凤); Tang GL(唐功利)
2014
发表期刊J. Am. Chem. Soc.
卷号136期号:12页码:4488-4491
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.
学科领域生命有机化学
DOI10.1021/ja500942y
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收录类别SCI
语种英语
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被引频次:15[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.sioc.ac.cn/handle/331003/38939
专题生命有机化学国家重点实验室
通讯作者Tang GL(唐功利)
作者单位中科院上海有机化学研究所
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GB/T 7714
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.
APA 贺海燕,唐满成,张凤,&唐功利.(2014).Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis.J. Am. Chem. Soc.,136(12),4488-4491.
MLA 贺海燕,et al."Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis".J. Am. Chem. Soc. 136.12(2014):4488-4491.
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