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NADP(+)-dependent isocitrate dehydrogenase from a psychrophilic bacterium, Psychromonas marina

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タイトル: NADP(+)-dependent isocitrate dehydrogenase from a psychrophilic bacterium, Psychromonas marina
著者: Hirota, Ryo 著作を一覧する
Tsubouchi, Kango 著作を一覧する
Takada, Yasuhiro 著作を一覧する
キーワード: Isocitrate dehydrogenase
Cold-adapted enzyme
Chimeric enzymes
Psychrophilic bacterium
Psychromonas marina
発行日: 2017年 7月
出版者: Springer
誌名: Extremophiles
巻: 21
号: 4
開始ページ: 711
終了ページ: 721
出版社 DOI: 10.1007/s00792-017-0936-0
PMID: 28447265
抄録: The gene encoding NADP+-dependent isocitrate dehydrogenase (IDH; EC of a psychrophilic bacterium, Psychromonas marina, was cloned and sequenced. The open reading frame of the gene encoding IDH of P. marina (PmIDH) was 2229 bp in length and corresponded to a polypeptide composed of 742 amino acids. The molecular mass of IDH was calculated as 80,426 Da. The deduced amino acid sequence of PmIDH exhibited high degrees of homology with the monomeric IDH from other bacteria such as Colwellia maris (62% identity) and Azotobacter vinelandii (AvIDH) (64%). His-tagged PmIDH overexpressed in Escherichia coli cells was purified and characterized. The optimum temperature of PmIDH activity was about 35 degrees C; however, the enzyme lost 74% of the activity after incubation for 10 min at 30 degrees C, indicating that this enzyme is thermolabile. Chimeric enzymes produced through domain swapping between PmIDH and mesophilic AvIDH were constructed and their optimum temperatures and thermostability were determined. The results suggest that regions 2 and 3, especially region 3, of the two IDHs are involved in their catalytic activities and optimum temperature and thermostability for activity.
Rights: The final publication is available at
資料タイプ: article (author version)
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 高田 泰弘


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