Purification and Properties of Phenylethylamine Oxidase of Arthrobacter globiformis

概要

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Phenylethylamine oxidase (EC class 1.4.3) of Arthrobacter globformis IFO 12137 (ATCC 8010) was purified to homogeneity. The enzyme had a M_r of 141,000 and was composed of two apparently identical subunits, which had a M_r of 71,000 and contained one copper ion. The absorption spectrum of the enzyme had maxima at 280 and 480nm, and the ratio A_<280>/A_<480> was 61,5. Hydrogen peroxide was formed in the oxidation of amines. The enzyme was most active and stable at pH 6.5. 2-Phenylethylamine and tyramine were the most actilve substrates. Several aromatic monoamines, aliphatic monoamines with 4-11 carbons, higher aliphatic diamines, and histamine were poor substrates. Benzylamine, putrescine, spermine, and spermidine were not oxidized. The K_ms for 2-phenylethylamine and tyramine were 18 and 85 μM, and the V_<max>s for them were 27.1 and 26.4 μmol/min/mg of enzyme, respectively. Benzyl alcohol was a non-competitive and benzylamine was a mix-type inhibitor of the enzyme. Carbonyl-blocking reagents such as methylhydrazine, Cu^<2+> -chelators, HgCl_2, p-chloromercuribenzoate, and Cl^- also inhibited the enzyme.
社団法人日本農芸化学会の論文
1997-03-23