PMID: 15388968Sep 25, 2004Paper

Purification and characterization of aromatic amine dehydrogenase from Alcaligenes xylosoxidans

Bioscience, Biotechnology, and Biochemistry
Tetsuya KondoTokuji Ikeda

Abstract

Aromatic amine dehydrogenase was purified and characterized from Alcaligenes xylosoxidans IFO13495 grown on beta-phenylethylamine. The molecular mass of the enzyme was 95.5 kDa. The enzyme consisted of heterotetrameric subunits (alpha2beta2) with two different molecular masses of 42.3 kDa and 15.2 kDa. The N-terminal amino acid sequences of the alpha-subunit (42.3-kDa subunit) and the beta-subunit (15.2-kDa subunit) were DLPIEELXGGTRLPP and APAAGNKXPQMDDTA respectively. The enzyme had a quinone cofactor in the beta-subunit and showed a typical absorption spectrum of tryptophan tryptophylquinone-containing quinoprotein showing maxima at 435 nm in the oxidized form and 330 nm in the reduced form. The pH optima of the enzyme activity for histamine, tyramine, and beta-phenylethylamine were the same at 8.0. The enzyme retained full activity after incubation at 70 degrees C for 40 min. It readily oxidized various aromatic amines as well as some aliphatic amines. The Michaelis constants for phenazine methosulfate, beta-phenylethylamine, tyramine, and histamine were 48.1, 1.8, 6.9, and 171 microM respectively. The enzyme activity was strongly inhibited by carbonyl reagents. The enzyme could be stored without appreciable loss of enzyme ...Continue Reading

References

Jan 1, 1983·Archives of Biochemistry and Biophysics·M IwakiM Nozaki

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Citations

Feb 19, 2016·Food Additives & Contaminants. Part A, Chemistry, Analysis, Control, Exposure & Risk Assessment·Ying XuWei Jiang
Sep 9, 2017·Journal of Food Protection·Hsien-Feng KungYung-Hsiang Tsai
Apr 16, 2020·Critical Reviews in Food Science and Nutrition·Yanshun XuWenshui Xia
Dec 1, 2015·Journal of Food and Drug Analysis·Yi-Chen LeeYung-Hsiang Tsai

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