Structural Insight into Acyl-ACP Thioesterase toward Substrate Specificity Design
文献类型：期刊论文
| 作者 | Liu, Yinghui1; Xue, Song1; Feng, Yanbin1; Wang, Yayue1,2; Liu, Jiao1,2; Cao, Xupeng1 |
| 刊名 | ACS CHEMICAL BIOLOGY
 |
| 出版日期 | 2017-11-01 |
| 卷号 | 12期号:11页码:2830-2836 |
| ISSN号 | 1554-8929 |
| DOI | 10.1021/acschembio.7b00641 |
| 文献子类 | Article |
| 英文摘要 | Acyl-ACP thioesterase (TE) catalyzes the hydrolysis of thioester bonds during type II fatty acid synthesis and directly determines fatty acid chain length. Most TEs are responsible for recognition of 16:0 and 18:1 substrates, while specific TEs interrupt acyl-ACP elongation at C8C14. However, the acyl selection mechanism of TE has not been thoroughly elucidated to date. In this study, the crystal structure of the C12-specific thioesterase FatB from Umbellularia californica, which consists of two independent hotdog domains, was determined. An uncanonical Asp-His-Glu catalytic network was identified on the C-terminal hotdog domain, whereas the substrate binding pocket was determined to be on the N-terminal hotdog domain. Moreover, we elucidated UcFatBs substrate selection mechanism, which is accommodated by several unconservative amino acids on the beta 5, beta 2, and beta 4 sheets and enclosed by T137 on the alpha 1 helix. On this basis, the C12-specific TE was rationally redesigned toward C14 selectivity by tuning the substrate binding pocket capacity. The T137G mutant demonstrated comparative relative activity on C14 substrates compared to C12 substrates in vitro. Furthermore, the reconstructed UcFatB_T137G achieved C14 fatty acid content up to 40% in contrast to 10% C14 from the wild type in engineered E. coli cells. The unraveled substrate selection mechanism of TE provides a new strategy for tailoring fatty acid synthesis. |
| WOS关键词 | FATTY-ACID BIOSYNTHESIS ; ESCHERICHIA-COLI ; CHEMICALS ; SYNTHETASE ; PLANTS ; FUELS |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000416204500016 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/169252]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 通讯作者 | Xue, Song |
| 作者单位 | 1.Chinese Acad Sci, Dalian Inst Chem Phys, Marine Bioengn Grp, Dalian 116023, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Yinghui,Xue, Song,Feng, Yanbin,et al. Structural Insight into Acyl-ACP Thioesterase toward Substrate Specificity Design[J]. ACS CHEMICAL BIOLOGY,2017,12(11):2830-2836. |
| APA | Liu, Yinghui,Xue, Song,Feng, Yanbin,Wang, Yayue,Liu, Jiao,&Cao, Xupeng.(2017).Structural Insight into Acyl-ACP Thioesterase toward Substrate Specificity Design.ACS CHEMICAL BIOLOGY,12(11),2830-2836. |
| MLA | Liu, Yinghui,et al."Structural Insight into Acyl-ACP Thioesterase toward Substrate Specificity Design".ACS CHEMICAL BIOLOGY 12.11(2017):2830-2836. |
入库方式： OAI收割
来源：大连化学物理研究所
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