Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme

被引：119

作者：

Requena, L ^{[1
]}

Bornemann, S ^{[1
]}

机构：

[1] John Innes Ctr Plant Sci Res, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

来源：

BIOCHEMICAL JOURNAL | 1999年 / 343卷

关键词：

EPR; germin; homology model; hydrogen peroxide;

D O I：

10.1042/0264-6021:3430185

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：

Oxalate oxidase (EC 1.2.3.4) catalyses the conversion of oxalate and dioxygen into CO2 and H2O2. The barley (Hordeum vulgare) seedling root enzyme was purified to homogeneity and shown by metal analysis and EPR spectroscopy to contain Mn(II) at up to 0.80 atom per subunit. The involvement of Mn and neither flavin, Cu nor Fe in the direct conversion of dioxygen to H2O2 makes oxalate oxidase unique. A model of the active site of the holoenzyme based on a homology model of the apoenzyme is proposed.

引用

页码：185 / 190

页数：6

共 35 条

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