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学科主题: 物理化学
题名: Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide
作者: Ji, Debin1, 2;  Wang, Lei1, 2;  Hou, Shuhua1, 2;  Liu, Wujun1, 3;  Wang, Jinxia1;  Wang, Qian1, 3;  Zhao, Zongbao K.1, 3
通讯作者: 赵宗保
刊名: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
发表日期: 2011-12-28
DOI: 10.1021/ja2074032
卷: 133, 期:51, 页:20857-20862
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1816
产权排名: 1,1
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Multidisciplinary
摘要: Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide
研究领域[WOS]: Chemistry
英文摘要: 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.
关键词[WOS]: ESCHERICHIA-COLI ;  DIRECTED EVOLUTION ;  NAD(+) TRANSPORTER ;  XYLOSE REDUCTASE ;  SMALL MOLECULES ;  SWISS-MODEL ;  SPECIFICITY ;  ENZYMES ;  BINDING ;  PROTEIN
语种: 英语
WOS记录号: WOS:000298571600037
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/115835
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.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:
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.
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