Barley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme.
Oxalate oxidase (EC 1.2.3.4) catalyses the conversion of oxalate and dioxygen into CO(2) and H(2)O(2). 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 H(2)O(2) makes oxalate oxidase unique. A model of the active site of the holoenzyme based on a homology model of the apoenzyme is proposed.
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Biological Chemistry Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, U.K.
Bornemann
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D001665:Binding Sites; D002240:Carbohydrate Sequence; D002384:Catalysis; D004578:Electron Spin Resonance Spectroscopy; D001467:Hordeum / Q000201:enzymology*; D008345:Manganese / Q000032:analysis*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013056:Spectrophotometry, Ultraviolet
D008345:Manganese; D010088:Oxidoreductases; C020598:oxalate oxidase