Characterization of a new enzyme oxidizing ω-amino group of aminocarboxyric acid, aminoalcohols and amines from Phialemonium sp. AIU 274

• A new enzyme, which oxidizes a wide variety of ω-amino compounds, was found from Phialemonium sp. AIU 274.
• The enzyme was specific to ω-amino compounds, and did not oxidize l- and d-amino acids.
• The enzyme preferably oxidized medium- and long-chain ω-amino compounds to the corresponding aldehyde compounds.
• The enzyme contained copper, and the enzyme activity was inhibited by isoniazid, iproniazid and semicarbazide.

A new enzyme exhibiting oxidase activity for ω-aminocarboxylic acids, ω-aminoalcohols, monoamines and diamines was found from a newly isolated fungal strain, Phialemonium sp. AIU 274. The enzyme also oxidized aromatic amines, but not l- and d-amino acids. The Vmax/Km value for hexylamine was higher than those for 6-aminoalcohol and 6-aminhexanoic acid in the aliphatic C6 substrates. In the aliphatic amines, the higher Vmax/Km values were obtained by the longer carbon chain amines. Thus, the enzyme catalyzed oxidative deamination of the ω-amino group in a wide variety of the ω-amino compounds and preferred medium- and long-chain substrates. The oxidase with such broad substrate specificity was first reported here. The enzyme contained copper, and the enzyme activity was strongly inhibited by isoniazid, iproniazid and semicarbazide, but not by clorgyline and pargyline. The enzyme was composed of two identical subunits of 75 kDa.

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