Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis

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	Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis
	He HY(贺海燕); Tang MC(唐满成); Zhang F(张凤); Tang GL(唐功利)
刊名	J. Am. Chem. Soc.
	2014
卷号	136 期号:12 页码:4488-4491
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
通讯作者	唐功利
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.
学科主题	生命有机化学
收录类别	SCI
原文出处	http://dx.doi.org/10.1021/ja500942y
语种	英语
内容类型	期刊论文
源URL	[http://ir.sioc.ac.cn/handle/331003/38939]
专题	上海有机化学研究所_生命有机化学国家重点实验室
作者单位	中科院上海有机化学研究所
推荐引用方式 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.