Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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An L-amino acid oxidase was found from a newly isolated strain, Pseudomonas sp. AIU 813. This enzyme was remarkably induced by incubation with L-lysine as a nitrogen source, and efficiently purified using an affinity chromatography with L-lysine as ligand. The enzyme oxidized L-lysine, L-ornithine and L-arginine, but not other L-amino acids and D-amino acids. The oxidase activity for L-lysine was detected in a wide pH range, and its optimal was pH 7.0. In contrast, the oxidase activity for L-ornithine and L-arginine was not shown in acidic region from pH 6.5, and optimal pH for both substrates was 9.0. The enzyme was a flavoprotein and composed of two identical subunits with molecular mass of 54.5 kDa. The N-terminal amino acid sequence was similar to that of putative fiavin-containing amine oxidase and putative tryptophan 2-monooxygenase, but not to that of L-amino acid oxidases.
著者
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Isobe Kimiyasu
Department Of Agro-bioscience Faculty Of Agriculture Iwate University
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Asano Yasuhisa
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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Asano Yasuhisa
Biotechnology Research Center And Department Of Biotechnology Toyama Prefectural University
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Fukuta Yasuhisa
Biotechnology Research Center And Department Of Biotechnology Toyama Prefectural University
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Isobe Kimiyasu
Department Of Biological Chemistry And Food Science Faculty Of Agriculture Iwate University
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Sugawara Asami
Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University
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Domon Hanako
Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University
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Sugawara Asami
Department Of Biological Chemistry And Food Science Faculty Of Agriculture Iwate University
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Domon Hanako
Department Of Biological Chemistry And Food Science Faculty Of Agriculture Iwate University
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