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 › peer-review

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

ASJC Scopus subject areas

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

Access to Document

10.1271/bbb1961.48.2549

Cite this

@article{4bf5a72e1ee24e0c8f2a37b35258c8b8,

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

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.",

author = "Toshiko Kido and Katsuyuki Tanizawa and Kenji Inagaki and Tohru Yoshimura and Masaaki Ishida and Katsumi Hashizume and Kenji Soda",

year = "1984",

doi = "10.1271/bbb1961.48.2549",

language = "English",

volume = "48",

pages = "2549--2554",

journal = "Agricultural and Biological Chemistry",

issn = "0002-1369",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "10",

}

TY - JOUR

T1 - 2-Nitropropane Dioxygenase from Hansenula mrakii

T2 - Re-characterization of the Enzyme and Oxidation of Anionic Nitroalkanes

AU - Kido, Toshiko

AU - Tanizawa, Katsuyuki

AU - Inagaki, Kenji

AU - Yoshimura, Tohru

AU - Ishida, Masaaki

AU - Hashizume, Katsumi

AU - Soda, Kenji

PY - 1984

Y1 - 1984

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=85007975042&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85007975042&partnerID=8YFLogxK

U2 - 10.1271/bbb1961.48.2549

DO - 10.1271/bbb1961.48.2549

M3 - Article

SN - 0002-1369

VL - 48

SP - 2549

EP - 2554

JO - Agricultural and Biological Chemistry

JF - Agricultural and Biological Chemistry

IS - 10

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this