CAS OpenIR  > 生化工程国家重点实验室
Stereospecificity of Enoylreductase Domains from Modular Polyketide Synthases
Zhang, Luyun1,2; Ji, Junjie3; Yuan, Meijuan1,2; Feng, Yuanyuan1,2; Wang, Lei1,2; Deng, Zixin1,2; Bai, Linquan1,2; Zheng, Jianting1,2
2018-04-01
Source PublicationACS CHEMICAL BIOLOGY
ISSN1554-8929
Volume13Issue:4Pages:871-875
AbstractAn enoylreductase (ER) domain of a polyketide synthase module recruiting a methylmalonate extender unit sets the C2 methyl branch to either the S or R configuration during processing of a polyketide intermediate carried by an acyl carrier protein (ACP) domain. In the present study, pantetheine- and ACP-bound trans-2-methylcrotonyl substrate surrogates were used to scrutinize the stereospecificity of the ER domains. The pantetheine-bound thioester was reduced to mixtures of both 2R and 2S products, whereas the expected 2S epimer was almost exclusively generated when the cognate ACP-bound substrate surrogate was utilized. The analogous incubation of an ER with the substrate surrogate carried by a noncognate ACP significantly increased the generation of the unexpected 2R epimer, highlighting the dependence of stereospecificity on proper protein protein interactions between ER and ACP domains. The ER mutant assays revealed the involvement of the conserved tyrosine and lysine in stereocontrol. Taken together, these results expand the current understanding of the ER stereochemistry and help in the engineering of modular PKSs.
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1021/acschembio.7b00982
Indexed BySCI
Language英语
WOS KeywordKETOREDUCTASE DOMAINS ; CARRIER PROTEIN ; STEREOCHEMISTRY ; BIOSYNTHESIS ; CATALYSIS ; ACYLTRANSFERASE ; MUTAGENESIS ; SUBSTRATE
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
Funding OrganizationNational Natural Science Foundation of China(31370101 ; National Program on Key Basic Research Project (973 program)(2013CB734002) ; State Key Laboratory of Pathogen and Biosecurity (Academy of Military Medical Science)(SKLPBS1526) ; Fundamental Research Funds for the Central Universities ; Global Talents Recruitment Program ; 31570056 ; 31770068)
WOS IDWOS:000430898600004
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/24436
Collection生化工程国家重点实验室
Affiliation1.Shanghai Jiao Tong Univ, State Key Lab Microbial Metab, Shanghai 200240, Peoples R China
2.Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, Shanghai 200240, Peoples R China
3.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Zhang, Luyun,Ji, Junjie,Yuan, Meijuan,et al. Stereospecificity of Enoylreductase Domains from Modular Polyketide Synthases[J]. ACS CHEMICAL BIOLOGY,2018,13(4):871-875.
APA Zhang, Luyun.,Ji, Junjie.,Yuan, Meijuan.,Feng, Yuanyuan.,Wang, Lei.,...&Zheng, Jianting.(2018).Stereospecificity of Enoylreductase Domains from Modular Polyketide Synthases.ACS CHEMICAL BIOLOGY,13(4),871-875.
MLA Zhang, Luyun,et al."Stereospecificity of Enoylreductase Domains from Modular Polyketide Synthases".ACS CHEMICAL BIOLOGY 13.4(2018):871-875.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zhang, Luyun]'s Articles
[Ji, Junjie]'s Articles
[Yuan, Meijuan]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zhang, Luyun]'s Articles
[Ji, Junjie]'s Articles
[Yuan, Meijuan]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zhang, Luyun]'s Articles
[Ji, Junjie]'s Articles
[Yuan, Meijuan]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.