2-Nitropropane Dioxygenase from Hansenula mrakii : Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes
スポンサーリンク
概要
- 論文の詳細を見る
2-Nitropropane dioxygenase, purified to homogeneity by an improved method from a yeast, Hansenula mrakii, has a molecular weight of 42, 000, and consists of a single polypeptide. The enzyme contains 1 mol of FAD per mol of enzyme. The iron protein associated with previous preparations was removed by the present purification procedures. The enzyme catalyzes the oxygenative denitrification of anionic nitroalkanes much more effectively than that of the neutral ones with the optimum pH of 6.5. The Michaelis constants for the anionic substrates are as follows : 2-nitropropane, 1.61mM; 1-nitropropane, 3.23mM; nitroethane, 3.13mM, and 3-nitro-2-butanol, 0.59mM.
- 社団法人 日本農芸化学会の論文
著者
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Soda Kenji
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Inagaki Kenji
Laboratory Of Chemistry Seirei Christopher College Of Nursing
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Kido Toshiko
Laboratory Of Microbial Biochemistry Institute Of Chemical Research Kyoto University
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Yoshimura Tohru
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Tanizawa Katsuyuki
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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ISHIDA Masaaki
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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HASHIZUME Katsumi
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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INAGAKI Kenji
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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YOSHIMURA Tohru
Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University
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