Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH
文献类型：期刊论文
| 作者 | Liu, Bin1,2; Hou, Yan3,4; Wang, Xiaozheng5; Ma, Xiaofang1,2; Fang, Shiqi1,2; Huang, Tao1,2; Chen, Yanli1; Bai, Zhiqiang1,2 ; Lin, Shuangjun5; Zhang, Rundong3,4
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| 刊名 | ORGANIC & BIOMOLECULAR CHEMISTRY
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| 出版日期 | 2019-11-28 |
| 卷号 | 17期号:44页码:9605-9614 |
| ISSN号 | 1477-0520 |
| DOI | 10.1039/c9ob01996k |
| 通讯作者 | Lin, Shuangjun(linsj@sjtu.edu.cn) ; Zhang, Rundong(rundongzhang@scu.edu.cn) ; Hu, Kaifeng(kaifenghu@mail.kib.ac.rn) |
| 英文摘要 | Diverse derivatives of amino acids with different steric configurations are important biosynthetic building blocks. In biology, epimerization is an important way to generate steric diversity. MarH catalyzes the epimerization of the beta-position of (3R)-beta-methyl-indolepyruvate (MeInPy), forming (3S)-beta-MeInPy. Both compounds are derivatives of l-tryptophan (l-Trp) and are important precursors of bioactive natural products. Here, we report the crystal structures of MarH and the NMR structure of its complex with l-Trp, an analogue of its native substrate, (3R)-beta-MeInPy. Structural analysis and mutagenesis studies indicated that His25 acts as a base to remove H-beta and generate a planar carbanion intermediate, which is then putatively reprotonated on the opposite face by a water molecule to form (3S)-beta-MeInPy in a stereospecific manner. The details of beta-site isomerization at the atomic level provide deeper insights into the epimerization mechanism of MarH and will facilitate further enzyme design to extend the substrate scope. |
| WOS研究方向 | Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:000498709600006 |
| 源URL | [http://ir.kib.ac.cn/handle/151853/70684]  |
| 专题 | 昆明植物研究所_植物化学与西部植物资源持续利用国家重点实验室 |
| 通讯作者 | Lin, Shuangjun; Zhang, Rundong; Hu, Kaifeng |
| 作者单位 | 1.Chinese Acad Sci, Key Lab Phytochem & Plant Resources West China, Kunming Inst Bot, Kunming 650201, Yunnan, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Sichuan Univ, Dept Ophthalmol, State Key Lab Biotherapy, West China Hosp, Chengdu 610041, Sichuan, Peoples R China 4.Collaborat Innovat Ctr Biotherapy, Chengdu 610041, Sichuan, Peoples R China 5.Shanghai Jiao Tong Univ, State Key Lab Microbial Metab, Sch Life Sci & Biotechnol, Shanghai 200240, Peoples R China 6.Chengdu Univ Tradit Chinese Med, Innovat Inst Chinese Med & Pharm, Chengdu 611137, Sichuan, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Bin,Hou, Yan,Wang, Xiaozheng,et al. Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH[J]. ORGANIC & BIOMOLECULAR CHEMISTRY,2019,17(44):9605-9614. |
| APA | Liu, Bin.,Hou, Yan.,Wang, Xiaozheng.,Ma, Xiaofang.,Fang, Shiqi.,...&Hu, Kaifeng.(2019).Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH.ORGANIC & BIOMOLECULAR CHEMISTRY,17(44),9605-9614. |
| MLA | Liu, Bin,et al."Structural basis of the mechanism of beta-methyl epimerization by enzyme MarH".ORGANIC & BIOMOLECULAR CHEMISTRY 17.44(2019):9605-9614. |
入库方式： OAI收割
来源：昆明植物研究所
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