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ENZYME entry: EC 126.96.36.199
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|Xanthine + H(2)O + O(2) <=> urate + H(2)O(2)|
|FAD; Iron-sulfur; Mo-molybdopterin.
- Also oxidizes hypoxanthine, some other purines and pterins,
and aldehydes, but is distinct from EC 188.8.131.52.
- Under some conditions the product is mainly superoxide rather than
peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 O(2)(.-) + 2 H(+).
- The mammallian enzyme predominantly exists as an NAD-dependent
dehydrogenase (EC 184.108.40.206).
- During purification the enzyme is largely converted to the O(2)-
dependent xanthine oxidase form (EC 220.127.116.11).
- The conversion can be triggered by several mechanisms, including the
oxidation of cysteine thiols to form disulfide bonds (which can be
catalyzed by EC 18.104.22.168 in the presence of glutathione disulfide) or
limited proteolysis, which results in irreversible conversion.
- The conversion can also occur in vivo.
- Formerly EC 22.214.171.124 and EC 126.96.36.199.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
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entries corresponding to 1.17.3.-
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entries corresponding to 1.-.-.-