2-Nitropropane Dioxygenase from Hansenula mrakii: Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes

Toshiko Kido; Katsuyuki Tanizawa; Kenji Inagaki; Tohru Yoshimura; Masaaki Ishida; Katsumi Hashizume; Kenji Soda

doi:10.1271/bbb1961.48.2549

2-Nitropropane Dioxygenase from Hansenula mrakii: Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes

Toshiko Kido, Katsuyuki Tanizawa, Kenji Inagaki, Tohru Yoshimura, Masaaki Ishida, Katsumi Hashizume, Kenji Soda

Research output: Contribution to journal › Article

18 Citations (Scopus)

Abstract

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, 1.61 mM; 1-nitropropane, 3.23 mM; nitroethane, 3.13 mM, and 3-nitro-2-butanol, 0.59 mM.

Original language	English
Pages (from-to)	2549-2554
Number of pages	6
Journal	Agricultural and Biological Chemistry
Volume	48
Issue number	10
DOIs	https://doi.org/10.1271/bbb1961.48.2549
Publication status	Published - 1984
Externally published	Yes

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ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)

Cite this

Kido, T., Tanizawa, K., Inagaki, K., Yoshimura, T., Ishida, M., Hashizume, K., & Soda, K. (1984). 2-Nitropropane Dioxygenase from Hansenula mrakii: Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes. Agricultural and Biological Chemistry, 48(10), 2549-2554. https://doi.org/10.1271/bbb1961.48.2549

2-Nitropropane Dioxygenase from Hansenula mrakii : Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes. / Kido, Toshiko; Tanizawa, Katsuyuki; Inagaki, Kenji; Yoshimura, Tohru; Ishida, Masaaki; Hashizume, Katsumi; Soda, Kenji.

In: Agricultural and Biological Chemistry, Vol. 48, No. 10, 1984, p. 2549-2554.

Research output: Contribution to journal › Article

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abstract = "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, 1.61 mM; 1-nitropropane, 3.23 mM; nitroethane, 3.13 mM, and 3-nitro-2-butanol, 0.59 mM.",

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AU - Soda, Kenji

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AB - 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, 1.61 mM; 1-nitropropane, 3.23 mM; nitroethane, 3.13 mM, and 3-nitro-2-butanol, 0.59 mM.

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10.1271/bbb1961.48.2549