HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science / Faculty of Science >
Peer-reviewed Journal Articles, etc >

Analysis of amino acid residues involved in cold activity of monomeric isocitrate dehydrogenase from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea

Files in This Item:
takada.pdf2.52 MBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/54722

Title: Analysis of amino acid residues involved in cold activity of monomeric isocitrate dehydrogenase from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea
Authors: Yasuda, Wataru Browse this author
Kobayashi, Miyuki Browse this author
Takada, Yasuhiro Browse this author →KAKEN DB
Keywords: Isocitrate dehydrogenase
Cold-adapted enzyme
Site-directed mutagenesis
Colwellia maris
Colwellia psychrerythraea
Issue Date: Nov-2013
Publisher: Soc bioscience bioengineering japan
Journal Title: Journal of bioscience and bioengineering
Volume: 116
Issue: 5
Start Page: 567
End Page: 572
Publisher DOI: 10.1016/j.jbiosc.2013.05.012
PMID: 23830032
Abstract: Monomeric isocitrate dehydrogenases from psychrophilic bacteria, Colwellia maris and Colwellia psychrerythraea (CmIDH-II and CpIDH-M, respectively) are cold-adapted enzymes and show a high degree of amino acid sequential identity to each other (77%). However, maximum activity of CpIDH-M at optimum temperature is much less than that of CmIDH-II. In the C-terminal region 3 of these enzymes, which was suggested from previous study to be responsible for their distinct catalytic ability, several sequential differences of amino acid residue are present. Among them, ten amino acid residues were exchanged between them by site-directed mutagenesis and several properties of the mutated enzymes were examined in this study. The mutated enzymes of CmIDH-II substituted its Gln671, Leu724 and Phe735 residues with the corresponding residues of CpIDH-M (termed Q671K, L724Q and F735L, respectively) showed lower specific activity and thermostability for activity than the wild-type enzyme. Furthermore, the decreased specific activity was also observed in L693F. In contrast, the corresponding mutants of CpIDH-M, F693L, Q724L and L735F, showed the increased specific activity and thermostability for activity. The catalytic efficiency (K-cat/K-m) values of these mutated CmIDH-II and CpIDH-M were lower and higher than those of their wild-type IDHs, respectively. These results suggest that the Gln671, Leu693, Leu724 and Phe735 residues of CmIDH-II are important for exerting its high catalytic ability. (C) 2013, The Society for Biotechnology, Japan. All rights reserved.
Rights: © 2013 The Society for Biotechnology, Japan
Relation: http://www.sbj.or.jp/jbb/jbb_copyright.html
Type: article (author version)
URI: http://hdl.handle.net/2115/54722
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)

Submitter: 高田 泰弘

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University