Abstract
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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