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Our screening study yielded a copper amine oxidase (SrAOX) from Syncephalastrum racemosum, which showed much higher affinity and catalytic efficiency toward ethanolamine (EA) than any other amine oxidase (AOX). Following purification of the enzyme to electrophoretic homogeneity from a cell-free extract, the maximum activity toward EA was detected at pH 7.2-7.5 and 45 °C. The SrAOX complementary DNA (cDNA) was composed of a 2052-bp open reading frame encoding a 683-amino acid protein with a molecular mass of 77,162 Da. The enzyme functions as a homodimer. The deduced amino acid sequence of SrAOX showed 55.3 

作者:Yoshitaka, Hirano;Keisuke, Chonan;Kazutaka, Murayama;Shin-Ich, Sakasegawa;Hideyuki, Matsumoto;Daisuke, Sugimori

来源:Applied microbiology and biotechnology 2016 年 100卷 9期

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作者:
Yoshitaka, Hirano;Keisuke, Chonan;Kazutaka, Murayama;Shin-Ich, Sakasegawa;Hideyuki, Matsumoto;Daisuke, Sugimori
来源:
Applied microbiology and biotechnology 2016 年 100卷 9期
标签:
Characterization Cloning Cu amine oxidase Enzymatic determination of ethanolamine Heterologous expression Syncephalastrum racemosum
Our screening study yielded a copper amine oxidase (SrAOX) from Syncephalastrum racemosum, which showed much higher affinity and catalytic efficiency toward ethanolamine (EA) than any other amine oxidase (AOX). Following purification of the enzyme to electrophoretic homogeneity from a cell-free extract, the maximum activity toward EA was detected at pH 7.2-7.5 and 45 °C. The SrAOX complementary DNA (cDNA) was composed of a 2052-bp open reading frame encoding a 683-amino acid protein with a molecular mass of 77,162 Da. The enzyme functions as a homodimer. The deduced amino acid sequence of SrAOX showed 55.3