Purification and Properties of Phenylethylamine Oxidase of Arthrobacter globiformis
Purification and Properties of Phenylethylamine Oxidase of Arthrobacter globiformis
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球状节杆菌苯乙胺氧化酶的纯化及性质
DOI：
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发表时间：
1997
期刊：
影响因子：
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通讯作者：
T. Yorifuji
中科院分区：
文献类型：
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作者：
E. Shimizu;K. Ohta;S. Takayama;Y. Kitagaki;K. Tanizawa;T. Yorifuji
将球形节杆菌IFO 12137（ATCC 8010）的苯乙胺氧化酶（EC分类1.4.3）纯化至均一。该酶的Mr为141，000，由两个明显相同的亚基组成，其Mr为71，000，含有一个铜离子。该酶的最大吸收波长为280和480 nm，A280/A480为61.5。过氧化氢在胺的氧化中形成。该酶在pH6.5时活性最高，稳定性最好。2-苯乙胺和酪胺是最活跃的底物。几种芳香族单胺、具有4-11个碳的脂肪族单胺、高级脂肪族二胺和组胺是不良底物。苄胺、腐胺、精胺和亚精胺未被氧化。2-苯乙胺和酪胺的Km分别为18和85 μm，Vmax分别为27.1和26.4μmol/min/mg酶。苯甲醇为非竞争性抑制剂，苄胺为混合型抑制剂。羰基封闭试剂，如甲基肼，...
Phenylethylamine oxidase (EC class 1.4.3) of Arthrobacter globiformis 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 active 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 26.4μmol/min/mg of enzyme, respectively. Benzyl alcohol was a noncompetitive and benzylamine was a mix-type inhibitor of the enzyme. Carbonyl-blocking reagents such as methylhydrazine, ...