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Stereoselective catalysis controlled by a native leucine or variant isoleucine wing-gatekeeper in 2-haloacid dehalogenase

文献类型：期刊论文

作者Cao, Xupeng1; Feng, Yanbin1; Wang, Yayue1,2; Chu, Huiying3; Fan, Yan1,4; Liu, Yinghui1; Li, Guohui3; Xue, Song1
刊名FEBS LETTERS
出版日期2019-02-01
卷号593期号:3页码:308-318
ISSN号1873-3468
关键词biocatalyst enzyme molecular dynamics protein engineering stereoselectivity
DOI10.1002/1873-3468.13309
通讯作者Li, Guohui(ghli@dicp.ac.cn) ; Xue, Song(xuesong@dicp.ac.cn)
英文摘要Comprehensively understanding enzymatic stereoselectivity will assist in the creation of new enzymes for producing optically pure compounds for chemical applications. The essential features for selecting enantiomers are controlled by particular residues or regions of the enzymes. We report a stereoselective mechanism in the D-2-haloacid dehalogenase HadD AJ1, in which L288 is identified as a gatekeeper in the access channel that strictly recognizes D-enantiomers. Mutagenesis of L288 to isoleucine (I) enlarges the size of the channel and allows the enzyme to accommodate L-enantiomers. Furthermore, the wing flip of I288 induces hydrophobic interactions with the L-enantiomer and directly affects the catalytic efficiency. The results illustrate the dynamic catalytic mechanisms of Leu-Ile gatekeepers and provide knowledge for unveiling the basis of stereospecificity in biocatalysts.
WOS关键词DL-2-HALOACID DEHALOGENASE ; HALOALKANE-DEHALOGENASE ; CRYSTAL-STRUCTURE ; ACTIVE-SITE ; ENANTIOSELECTIVITY ; ENZYMES ; REVEAL ; TUNNEL
资助项目National Natural Science Foundation of China[21576253] ; National Natural Science Foundation of China[31500294] ; National Natural Science Foundation of China[21708040]
WOS研究方向Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
语种英语
出版者WILEY
WOS记录号WOS:000458335400005
资助机构National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China
源URL[http://cas-ir.dicp.ac.cn/handle/321008/166136]  
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Li, Guohui; Xue, Song
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Shangqiu Normal Univ, Sch Biol & Food Sci, Shangqiu, Peoples R China
3.Chinese Acad Sci, Lab Mol Modeling & Design, State Key Lab Mol React Dynam, Dalian Inst Chem Phys, Dalian, Peoples R China
4.Univ Chinese Acad Sci, Beijing, Peoples R China
推荐引用方式
GB/T 7714		 Cao, Xupeng,Feng, Yanbin,Wang, Yayue,et al. Stereoselective catalysis controlled by a native leucine or variant isoleucine wing-gatekeeper in 2-haloacid dehalogenase[J]. FEBS LETTERS,2019,593(3):308-318.
APA Cao, Xupeng.,Feng, Yanbin.,Wang, Yayue.,Chu, Huiying.,Fan, Yan.,...&Xue, Song.(2019).Stereoselective catalysis controlled by a native leucine or variant isoleucine wing-gatekeeper in 2-haloacid dehalogenase.FEBS LETTERS,593(3),308-318.
MLA Cao, Xupeng,et al."Stereoselective catalysis controlled by a native leucine or variant isoleucine wing-gatekeeper in 2-haloacid dehalogenase".FEBS LETTERS 593.3(2019):308-318.

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来源：大连化学物理研究所

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