Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase
文献类型：期刊论文
| 作者 | Feng, Yanbin2; Guo, Xiaojia1,2; Wang, Xueying2; Liu, Yuxue1,2; Liu, Wujun2; Li, Qing1,2; Wang, Junting1,2; Xue, Song2; Zhao, Zongbao K.2 |
| 刊名 | BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
 |
| 出版日期 | 2019-06-15 |
| 卷号 | 29期号:12页码:1446-1449 |
| ISSN号 | 0960-894X |
| 关键词 | Alcohol dehydrogenase Substrate preference Methanol dehydrogenase Geobacillus stearothermophilus Molecular docking Cofactor regeneration |
| DOI | 10.1016/j.bmcl.2019.04.025 |
| 通讯作者 | Zhao, Zongbao K.(zhaozb@dicp.ac.cn) |
| 英文摘要 | Many alcohol dehydrogenases (ADHs) catalyze oxidation of a broad scope of alcohols. When an NAD-dependent ADH oxidizes methanol, albeit at a poor rate, it may be treated as methanol dehydrogenase (MDH). One ADH from Geobacillus stearothermophilus DSM 2334 (GsADH) has been widely used as MDH, but its actual substrate scope remains less characterized. Here we purified recombinant GsADH from Escherichia coli and determined its crystal structure. We collected kinetics data of this enzyme towards a number of short chain alcohols, and found that isopropanol is by far the most favorable substrate. Moreover, molecular docking analysis suggested that substrate preference is mainly attributed to the conformer energy of the protein-substrate complex. Our data clarified the substrate scope of GsADH and provided structural insights, which may facilitate more efficient cofactor regeneration and rational metabolic engineering. |
| WOS关键词 | BACILLUS-STEAROTHERMOPHILUS ; NADH ; REDUCTION ; COMPLEX ; SYSTEM |
| 资助项目 | National Natural Science Foundation of China, China[21877112] ; National Natural Science Foundation of China, China[21721004] ; Dalian Institute of Chemical Physics, CAS, China[DMTO201701] |
| WOS研究方向 | Pharmacology & Pharmacy ; Chemistry |
| 语种 | 英语 |
| 出版者 | PERGAMON-ELSEVIER SCIENCE LTD |
| WOS记录号 | WOS:000466365200003 |
| 资助机构 | National Natural Science Foundation of China, China ; National Natural Science Foundation of China, China ; Dalian Institute of Chemical Physics, CAS, China ; Dalian Institute of Chemical Physics, CAS, China ; National Natural Science Foundation of China, China ; National Natural Science Foundation of China, China ; Dalian Institute of Chemical Physics, CAS, China ; Dalian Institute of Chemical Physics, CAS, China ; National Natural Science Foundation of China, China ; National Natural Science Foundation of China, China ; Dalian Institute of Chemical Physics, CAS, China ; Dalian Institute of Chemical Physics, CAS, China ; National Natural Science Foundation of China, China ; National Natural Science Foundation of China, China ; Dalian Institute of Chemical Physics, CAS, China ; Dalian Institute of Chemical Physics, CAS, China |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/165514]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 通讯作者 | Zhao, Zongbao K. |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China |
| 推荐引用方式 GB/T 7714 | Feng, Yanbin,Guo, Xiaojia,Wang, Xueying,et al. Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase[J]. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS,2019,29(12):1446-1449. |
| APA | Feng, Yanbin.,Guo, Xiaojia.,Wang, Xueying.,Liu, Yuxue.,Liu, Wujun.,...&Zhao, Zongbao K..(2019).Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase.BIOORGANIC & MEDICINAL CHEMISTRY LETTERS,29(12),1446-1449. |
| MLA | Feng, Yanbin,et al."Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase".BIOORGANIC & MEDICINAL CHEMISTRY LETTERS 29.12(2019):1446-1449. |
入库方式： OAI收割
来源：大连化学物理研究所
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