Cis-Double Bond Formation by Thioesterase and Transfer by Ketosynthase in FR901464 Biosynthesis
文献类型：期刊论文
| 作者 | 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.
 |
| 出版日期 | 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 |
| 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. |
入库方式： OAI收割
来源：上海有机化学研究所
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