DICP OpenIR
Stereoselective catalysis controlled by a native leucine or variant isoleucine wing-gatekeeper in 2-haloacid dehalogenase
Feng, Yanbin1; Wang, Yayue1,2; Chu, Huiying3; Fan, Yan1,4; Cao, Xupeng1; Liu, Yinghui1; Li, Guohui3; Xue, Song1
Corresponding AuthorLi, Guohui(ghli@dicp.ac.cn) ; Xue, Song(xuesong@dicp.ac.cn)
Keywordbiocatalyst enzyme molecular dynamics protein engineering stereoselectivity
Source PublicationFEBS LETTERS
2019-02-01
ISSN1873-3468
DOI10.1002/1873-3468.13309
Volume593Issue:3Pages:308-318
Funding ProjectNational Natural Science Foundation of China[21576253] ; National Natural Science Foundation of China[31500294] ; National Natural Science Foundation of China[21708040]
Funding OrganizationNational 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
WOS SubjectBiochemistry & Molecular Biology ; Biophysics ; Cell Biology
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics ; Cell Biology
WOS KeywordDL-2-HALOACID DEHALOGENASE ; HALOALKANE-DEHALOGENASE ; CRYSTAL-STRUCTURE ; ACTIVE-SITE ; ENANTIOSELECTIVITY ; ENZYMES ; REVEAL ; TUNNEL
AbstractComprehensively 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.
Language英语
Funding OrganizationNational 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
WOS IDWOS:000458335400005
PublisherWILEY
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/166137
Collection中国科学院大连化学物理研究所
Corresponding AuthorLi, Guohui; Xue, Song
Affiliation1.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
Recommended Citation
GB/T 7714
Feng, Yanbin,Wang, Yayue,Chu, Huiying,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 Feng, Yanbin.,Wang, Yayue.,Chu, Huiying.,Fan, Yan.,Cao, Xupeng.,...&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 Feng, Yanbin,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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