Purification, Characterization, and Overexpression of Psychrophilic and Thermolabile Malate Dehydrogenase of a Novel Antarctic Psychrotolerant, Flavobacterium frigidimaris KUC-1
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概要
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We purified the psychrophilic and thermolabile malate dehydrogenase to homogeneity from a novel psychrotolerant, Flavobacterium frigidimaris KUC-1, isolated from Antarctic seawater. The enzyme was a homotetramer with a molecular weight of about 123 k and that of the subunit was about 32 k. The enzyme required NAD(P)+ as a coenzyme and catalyzed the oxidation of L-malate and the reduction of oxalacetate specifically. The reaction proceeded through an ordered bi–bi mechanism. The enzyme was highly susceptible to heat treatment, and the half-life time at 40 °C was estimated to be 3.0 min. The kcat⁄Km (μM−1·s−1) values for L-malate and NAD+ at 30 °C were 289 and 2,790, respectively. The enzyme showed pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. The enzyme contained 311 amino acid residues and much lower numbers of proline and arginine residues than other malate dehydrogenases.
- 社団法人 日本農芸化学会の論文
- 2005-11-23
著者
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Yamamoto Noriko
Department of Cell Regeneration and Transplantation, Nihon University School of Medicine
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UESATO Shinichi
Department of Biotechnology, Faculty of Engineering, Kansai University
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OIKAWA Tadao
Department of Pediatrics, National Tochigi Hospital
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Uesato Shinichi
Department Of Life Science And Biotechnology Faculty Of Chemistry Materials And Bioengineering Kansa
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Uesato Shinichi
Department Of Biotechnology Faculty Of Engineering Kansai Univeristy
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Yamamoto Noriko
Department Of Biotechnology Faculty Of Engineering Kansai University
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Oikawa Tadao
Department Of Biotechnology Kansai University
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Oikawa Tadao
Kansai University
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Shimoke Koji
Department Of Life Science And Biotechnology Faculty Of Chemistry Materials And Bioengineering Kansa
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FUJIOKA Toru
Department of Obstetrics and Gynecology, Ehime University Graduate School of Medicine
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Fujioka Toru
Department Of Biotechnology Faculty Of Engineering Kansai University
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SHIMOKE Koji
Kansai University High Technology Research Center
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IKEUCHI Toshihiko
Kansai University High Technology Research Center
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Yamamoto Noriko
Department Of Biology Ochanomizu University
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Shimoke Koji
Kansai Univ. Osaka Jpn
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Oikawa Tadao
Department Of Biotechnology Faculty Of Engineering Kansai University
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Yamamoto Noriko
Department Of Biology Faculty Of Science And Engineering Konan University
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Yamamoto Noriko
Department Of Applied Chemistry Faculty Of Science And Technology Keio University
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