DICP OpenIR
Subject Area物理化学
Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide
Ji, Debin1,2; Wang, Lei1,2; Hou, Shuhua1,2; Liu, Wujun1,3; Wang, Jinxia1; Wang, Qian1,3; Zhao, Zongbao K.1,3; Zhao ZB(赵宗保)
Source PublicationJOURNAL OF THE AMERICAN CHEMICAL SOCIETY
2011-12-28
ISSN待补充
DOI10.1021/ja2074032
Volume133Issue:51Pages:20857-20862
Indexed BySCI
SubtypeArticle
Department18
Funding Project1816
Contribution Rank1,1
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Multidisciplinary
WOS Research AreaChemistry
WOS KeywordESCHERICHIA-COLI ; DIRECTED EVOLUTION ; NAD(+) TRANSPORTER ; XYLOSE REDUCTASE ; SMALL MOLECULES ; SWISS-MODEL ; SPECIFICITY ; ENZYMES ; BINDING ; PROTEIN
AbstractCreation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide; Many enzymes catalyzing biological redox chemistry depend on the omnipresent cofactor, nicotinamide adenine dinucleotide (NAD). NAD is also involved in various nonredox processes. It remains challenging to disconnect one particular NAD-dependent reaction from all others. Here we present a bioorthogonal system that catalyzes the oxidative decarboxylation of L-malate with a dedicated abiotic cofactor, nicotinamide flucytosine dinucleotide (NFCD). By screening the multisite saturated mutagenesis libraries of the NAD-dependent malic enzyme (ME), we identified the mutant ME-L310R/Q401C, which showed excellent activity with NFCD, yet marginal activity with NAD. We found that another synthetic cofactor, nicotinamide cytosine dinucleotide (NCD), also displayed similar activity with the ME mutants. Inspired by these observations, we mutated D-lactate dehydrogenase (DLDH) and malate dehydrogenase (MDH) to DLDH-V152R and MDH-L6R, respectively, and both mutants showed fully active with NFCD. When coupled with DLDH-V152R, ME-L310R/Q401C required only a catalytic amount of NFCD to convert L-malate. Our results opened the window to engineer bioorthogonal redox systems for a wide variety of applications in systems biology and synthetic biology.
Language英语
WOS IDWOS:000298571600037
Citation statistics
Cited Times:35[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/115835
Collection中国科学院大连化学物理研究所
Corresponding AuthorZhao ZB(赵宗保)
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
3.Dalian Natl Lab Clean Energy, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Ji, Debin,Wang, Lei,Hou, Shuhua,et al. Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2011,133(51):20857-20862.
APA Ji, Debin.,Wang, Lei.,Hou, Shuhua.,Liu, Wujun.,Wang, Jinxia.,...&赵宗保.(2011).Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,133(51),20857-20862.
MLA Ji, Debin,et al."Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 133.51(2011):20857-20862.
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