DICP OpenIR
Structural Insights into Phosphite Dehydrogenase Variants Favoring a Non-natural Redox Cofactor
Liu, Yuxue1,2; Feng, Yanbin1; Wang, Lei1; Guo, Xiaojia1,2; Liu, Wujun1; Li, Qing1,2; Wang, Xueying1; Xue, Song1; Zhao, Zongbao Kent1,3
Corresponding AuthorXue, Song(xuesong@dicp.ac.cn) ; Zhao, Zongbao Kent(zhaozb@dicp.ac.cn)
Keywordphosphite dehydrogenase non-natural redox cofactor NAD-binding pocket nicotinamide cytosine dinucleotide cofactor preference
Source PublicationACS CATALYSIS
2019-03-01
ISSN2155-5435
DOI10.1021/acscatal.8b04822
Volume9Issue:3Pages:1883-1887
Funding ProjectNational Natural Science Foundation of China[21572227] ; National Natural Science Foundation of China[21778053] ; National Natural Science Foundation of China[21721004] ; Dalian Institute of Chemical Physics, CAS[DICPQIBEBT UN201706] ; Dalian Institute of Chemical Physics, CAS[DICP ZZBS201605]
Funding OrganizationNational Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS
WOS SubjectChemistry, Physical
WOS Research AreaChemistry
WOS KeywordEMISSIVE SYNTHETIC COFACTORS ; REGENERATION ; EVOLUTION ; NAD(+) ; ANALOGS ; NADH
AbstractImplementation of a non-natural cofactor alternative to the ubiquitous redox cofactor nicotinamide adenosine dinucleotide (NAD) is of great scientific and biotechnological interest. Several redox enzymes have been engineered to favor nicotinamide cytosine dinucleotide (NCD), a smaller-sized NAD analogue. However, molecular interactions involving NAD analogues remain elusive, preventing us from devising more enzymes to accept those analogues. Here we took a semirational approach to evolve phosphite dehydrogenase (Pdh) and identified variants with substantially improved NCD preference. These mutants are valuable components for regeneration of reduced NCD by using phosphite as the electron donor. We then collected X-ray crystal structures of three Pdh variants and their NCD-complexes to delineate molecular basis for NCD binding. It was found that the incorporation of amino acid residues with large side chains enclosing the NAD-binding pocket led to compacted environment favoring NCD over NAD, and additional interactions between NCD and these side chains. These results guided successful engineering of more Pdh mutants with good NCD preference. As many redox enzymes share key structural features, our strategy may be readily adopted to devise NCD-favoring enzymes. We expected that, in the near future, more synthetic systems linked to non-natural cofactors will be created as alternative tools for widespread applications to address challenging problems by chemical and synthetic biologists.
Language英语
Funding OrganizationNational Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; Dalian Institute of Chemical Physics, CAS ; Dalian Institute of Chemical Physics, CAS
WOS IDWOS:000460600600025
PublisherAMER CHEMICAL SOC
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/165861
Collection中国科学院大连化学物理研究所
Corresponding AuthorXue, Song; Zhao, Zongbao Kent
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Div Biotechnol, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Catalysis, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Liu, Yuxue,Feng, Yanbin,Wang, Lei,et al. Structural Insights into Phosphite Dehydrogenase Variants Favoring a Non-natural Redox Cofactor[J]. ACS CATALYSIS,2019,9(3):1883-1887.
APA Liu, Yuxue.,Feng, Yanbin.,Wang, Lei.,Guo, Xiaojia.,Liu, Wujun.,...&Zhao, Zongbao Kent.(2019).Structural Insights into Phosphite Dehydrogenase Variants Favoring a Non-natural Redox Cofactor.ACS CATALYSIS,9(3),1883-1887.
MLA Liu, Yuxue,et al."Structural Insights into Phosphite Dehydrogenase Variants Favoring a Non-natural Redox Cofactor".ACS CATALYSIS 9.3(2019):1883-1887.
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