DICP OpenIR
学科主题物理化学
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)
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
2011-12-28
ISSN待补充
DOI10.1021/ja2074032
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
研究领域[WOS]Chemistry
关键词[WOS]ESCHERICHIA-COLI ; DIRECTED EVOLUTION ; NAD(+) TRANSPORTER ; XYLOSE REDUCTASE ; SMALL MOLECULES ; SWISS-MODEL ; SPECIFICITY ; ENZYMES ; BINDING ; PROTEIN
英文摘要Creation 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.
语种英语
WOS记录号WOS:000298571600037
引用统计
被引频次:30[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/115835
专题中国科学院大连化学物理研究所
通讯作者Zhao ZB(赵宗保)
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
推荐引用方式
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.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
2011V7UfdqIrUT.pdf(1004KB) 开放获取--请求全文
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Ji, Debin]的文章
[Wang, Lei]的文章
[Hou, Shuhua]的文章
百度学术
百度学术中相似的文章
[Ji, Debin]的文章
[Wang, Lei]的文章
[Hou, Shuhua]的文章
必应学术
必应学术中相似的文章
[Ji, Debin]的文章
[Wang, Lei]的文章
[Hou, Shuhua]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。