Structural insights into phosphite dehydrogenase variants favoring a non-natural redox cofactor
文献类型：期刊论文
| 作者 | Liu, Yuxue1,2; Feng, Yanbin1; Wang, Lei1; Guo, Xiaojia1,2; Liu, Wujun1; Li, Qing1,2; Wang, Xueying1; Xue, Song1; Zhao, Zongbao Kent1,3 |
| 刊名 | Acs catalysis
 |
| 出版日期 | 2019-03-01 |
| 卷号 | 9期号:3页码:1883-1887 |
| 关键词 | Phosphite dehydrogenase Non-natural redox cofactor Nad-binding pocket Nicotinamide cytosine dinucleotide Cofactor preference |
| ISSN号 | 2155-5435 |
| DOI | 10.1021/acscatal.8b04822 |
| 通讯作者 | Xue, song(xuesong@dicp.ac.cn) ; Zhao, zongbao kent(zhaozb@dicp.ac.cn) |
| 英文摘要 | Implementation 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. |
| WOS关键词 | EMISSIVE SYNTHETIC COFACTORS ; REGENERATION ; EVOLUTION ; NAD(+) ; ANALOGS ; NADH |
| WOS研究方向 | Chemistry |
| WOS类目 | Chemistry, Physical |
| 语种 | 英语 |
| WOS记录号 | WOS:000460600600025 |
| 出版者 | AMER CHEMICAL SOC |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2372700 |
| 专题 | 大连化学物理研究所 |
| 通讯作者 | Xue, Song; Zhao, Zongbao Kent |
| 作者单位 | 1.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 |
| 推荐引用方式 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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来源：大连化学物理研究所
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