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Characterization of NADP(+)-dependent isocitrate dehydrogenase isozymes from a psychrophilic bacterium, Colwellia psychrerythraea strain 34H
Title: | Characterization of NADP(+)-dependent isocitrate dehydrogenase isozymes from a psychrophilic bacterium, Colwellia psychrerythraea strain 34H |
Authors: | Suzuki, Kaori Browse this author | Takada, Yasuhiro Browse this author →KAKEN DB |
Keywords: | isocitrate dehydrogenase | isozymes | cold-adapted enzyme | Colwellia psychrerythraea strain 34H |
Issue Date: | Aug-2016 |
Publisher: | Taylor & Francis |
Journal Title: | Bioscience biotechnology and biochemistry |
Volume: | 80 |
Issue: | 8 |
Start Page: | 1492 |
End Page: | 1498 |
Publisher DOI: | 10.1080/09168451.2016.1165602 |
PMID: | 27033696 |
Abstract: | NADP(+)-dependent isocitrate dehydrogenase (IDH) isozymes of a psychrophilic bacterium, Colwellia psychrerythraea strain 34H, were characterized. The coexistence of monomeric and homodimeric IDHs in this bacterium was confirmed by Western blot analysis, the genes encoding two monomeric (IDH-IIa and IDH-IIb) and one dimeric (IDH-I) IDHs were cloned and overexpressed in Escherichia coli, and the three IDH proteins were purified. Both of the purified IDH-IIa and IDH-IIb were found to be cold-adapted enzymes while the purified IDH-I showed mesophilic properties. However, the specific activities of IDH-IIa and IDH-IIb were lower even at low temperatures than that of IDH-I. Therefore, IDH-I was suggested to be important for the growth of this bacterium. The results of colony formation of E. coli transformants carrying the respective IDH genes and IDH activities in their crude extracts indicated that the expression of the IDH-IIa gene is cold-inducible in the E. coli cells. |
Rights: | This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience, biotechnology, and biochemistry on 2016, available online: http://www.tandfonline.com/10.1080/09168451.2016.1165602. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/66934 |
Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 高田 泰弘
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