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.
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U2 - 10.1271/bbb1961.48.2549
DO - 10.1271/bbb1961.48.2549
M3 - Article
VL - 48
SP - 2549
EP - 2554
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 10
ER -