1997 Volume 61 Issue 3 Pages 501-505
Phenylethylamine oxidase (EC class 1.4.3) of Arthrobacter globformis IFO 12137 (ATCC 8010) was purified to homogeneity. The enzyme had a Mr of 141, 000 and was composed of two apparently identical subunits, which had a Mr of 71, 000 and contained one copper ion. The absorption spectrum of the enzyme had maxima at 280 and 480nm, and the ratio A280/A480 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 Kms for 2-phenylethylamine and tyramine were 18 and 85 μM, and the Vmaxs 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, Cu2+ -chelators, HgCl2, p-chloromercuribenzoate, and Cl- also inhibited the enzyme.
This article cannot obtain the latest cited-by information.
