Structural and Biochemical Analysis of Butanol Dehydrogenase From Thermotoga maritima.

Autor: Bai X; Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian, Liaoning, China.; Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian, China., Xu K; Department of Ophthalmology, The Fourth People's Hospital of Shenyang, Shenyang, China., Zhao Z; Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian, Liaoning, China.; Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian, China., Qin H; CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, Liaoning, China., Nam KH; College of General Education, Kookmin University, Seoul, South Korea., Quan C; Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian, Liaoning, China.; Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian, China., Ha NC; Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Seoul, South Korea., Xu Y; Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian, Liaoning, China.; Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian, China.
Jazyk: angličtina
Zdroj: Proteins [Proteins] 2024 Dec; Vol. 92 (12), pp. 1357-1365. Date of Electronic Publication: 2024 Jul 18.
DOI: 10.1002/prot.26731
Abstrakt: Butanol dehydrogenase (BDH) plays a crucial role in butanol biosynthesis by catalyzing the conversion of butanal to butanol using the coenzyme NAD(P)H. In this study, we observed that BDH from Thermotoga maritima (TmBDH) exhibits dual coenzyme specificity and catalytic activity with NADPH as the coenzyme under highly alkaline conditions. Additionally, a thermal stability analysis on TmBDH demonstrated its excellent activity retention even at elevated temperatures of 80°C. These findings demonstrate the superior thermal stability of TmBDH and suggest that it is a promising candidate for large-scale industrial butanol production. Furthermore, we discovered that TmBDH effectively catalyzes the conversion of aldehydes to alcohols and exhibits a wide range of substrate specificities toward aldehydes, while excluding alcohols. The dimeric state of TmBDH was observed using rapid online buffer exchange native mass spectrometry. Additionally, we analyzed the coenzyme-binding sites and inferred the possible locations of the substrate-binding sites. These results provide insights that improve our understanding of BDHs.
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Databáze: MEDLINE
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