Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity
文献类型：期刊论文
| 作者 | Yang, Jian; Xiao, Yun-Zhu; Li, Ru; Liu, Yu; Long, Li-Juan |
| 刊名 | BIOTECHNOLOGY AND BIOENGINEERING
 |
| 出版日期 | 2020 |
| 卷号 | 117期号:9页码:2694 |
| 关键词 | active-site reshaping catalytic selectivity enzyme promiscuity protein engineering substrate repositioning |
| ISSN号 | 0006-3592 |
| DOI | 10.1002/bit.27455 |
| 英文摘要 | Enzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions. |
| 资助机构 | Strategic Priority Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [XDA13020301]; Science and Technology Project of Guangzhou [201904010165]; Guangdong Natural Science FoundationNational Natural Science Foundation of Guangdong Province [2019A1515011629]; Key Special Project for Introduced Talents Team of Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou) [GML2019ZD0404]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [41406193]; Administration of Ocean and Fisheries of Guangdong Province [GD2012-D01-002] ; Strategic Priority Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [XDA13020301]; Science and Technology Project of Guangzhou [201904010165]; Guangdong Natural Science FoundationNational Natural Science Foundation of Guangdong Province [2019A1515011629]; Key Special Project for Introduced Talents Team of Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou) [GML2019ZD0404]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [41406193]; Administration of Ocean and Fisheries of Guangdong Province [GD2012-D01-002] |
| 源URL | [http://ir.scsio.ac.cn/handle/344004/18390]  |
| 专题 | 南海海洋研究所_中科院海洋生物资源可持续利用重点实验室 |
| 作者单位 | 1.Li, Ru 2.Xiao, Yun-Zhu 3.[Yang, Jian 4.Southern Marine Sci & Engn Guangdong Lab, Guangzhou, Peoples R China 5.Shenzhen Univ, Coll Life Sci & Oceanol, Shenzhen Key Lab Microbial Genet Engn, Shenzhen, Peoples R China 6.[Li, Ru 7.Liu, Yu 8.Univ Chinese Acad Sci, Beijing, Peoples R China 9.[Yang, Jian 10.Chinese Acad Sci, South China Sea Inst Oceanol, CAS Key Lab Trop Marine Bioresources & Ecol, Guangdong Key Lab Marine Mat Med, Guangzhou 510301, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Jian,Xiao, Yun-Zhu,Li, Ru,et al. Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity[J]. BIOTECHNOLOGY AND BIOENGINEERING,2020,117(9):2694, 2702. |
| APA | Yang, Jian,Xiao, Yun-Zhu,Li, Ru,Liu, Yu,&Long, Li-Juan.(2020).Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity.BIOTECHNOLOGY AND BIOENGINEERING,117(9),2694. |
| MLA | Yang, Jian,et al."Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity".BIOTECHNOLOGY AND BIOENGINEERING 117.9(2020):2694. |
入库方式： OAI收割
来源：南海海洋研究所
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