DICP OpenIR
Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase
Guo, Xiaojia1,2; Feng, Yanbin1; Wang, Xueying1; Liu, Yuxue1,2; Liu, Wujun1; Li, Qing1,2; Wang, Junting1,2; Xue, Song1; Zhao, Zongbao K.1
Corresponding AuthorZhao, Zongbao K.(zhaozb@dicp.ac.cn)
KeywordAlcohol dehydrogenase Substrate preference Methanol dehydrogenase Geobacillus stearothermophilus Molecular docking Cofactor regeneration
Source PublicationBIOORGANIC & MEDICINAL CHEMISTRY LETTERS
2019-06-15
ISSN0960-894X
DOI10.1016/j.bmcl.2019.04.025
Volume29Issue:12Pages:1446-1449
Funding ProjectNational Natural Science Foundation of China, China[21877112] ; National Natural Science Foundation of China, China[21721004] ; Dalian Institute of Chemical Physics, CAS, China[DMTO201701]
Funding OrganizationNational 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
WOS SubjectChemistry, Medicinal ; Chemistry, Organic
WOS Research AreaPharmacology & Pharmacy ; Chemistry
WOS KeywordBACILLUS-STEAROTHERMOPHILUS ; NADH ; REDUCTION ; COMPLEX ; SYSTEM
AbstractMany 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.
Language英语
Funding OrganizationNational 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
WOS IDWOS:000466365200003
PublisherPERGAMON-ELSEVIER SCIENCE LTD
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/165515
Collection中国科学院大连化学物理研究所
Corresponding AuthorZhao, Zongbao K.
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Guo, Xiaojia,Feng, Yanbin,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 Guo, Xiaojia.,Feng, Yanbin.,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 Guo, Xiaojia,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.
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