HISTAMINE OXIDASE, A CU2+-QUINOPROTEIN ENZYME OF ARTHROBACTER-GLOBIFORMIS

被引：16

作者：

SHIMIZU, E ^{[1
]}

ODAWARA, T ^{[1
]}

TANIZAWA, K ^{[1
]}

YORIFUJI, T ^{[1
]}

机构：

[1] OSAKA UNIV, INST SCI & IND RES, IBARAKI, OSAKA 567, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1994年 / 58卷 / 11期

关键词：

D O I：

10.1271/bbb.58.2118

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Histamine oxidase (EC class 1.4.3) was found in cells of Arthrobacter globiformis IFO 12137 (ATCC 8010) grown on histamine, The enzyme purified to a specific activity of 9.4 units/mg had a purity of at least 80%. The enzyme oxidized histamine with concomitant formation of H2O2. Phenylethylamine, dopamine, aromatic monoamines, and aliphatic mono- and diamines were oxidized at lower rates. Cu2+-chelators inhibited the enzyme, indicating that the enzyme is Cu2+-dependent. Carbonyl-blocking reagents also inhibited the enzyme. The enzyme catalyzed the Nitro Blue Tetrazolium/glycinate reaction, which is characteristically catalyzed by quinones and quinoproteins. These results strongly suggest that the enzyme contains a quinonoid cofactor.

引用

页码：2118 / 2120

页数：3

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