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ENZYME entry: EC 18.104.22.168
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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 22.214.171.124.
- 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 126.96.36.199).
- During purification the enzyme is largely converted to the O(2)-
dependent xanthine oxidase form (EC 188.8.131.52).
- The conversion can be triggered by several mechanisms, including the
oxidation of cysteine thiols to form disulfide bonds (which can be
catalyzed by EC 184.108.40.206 in the presence of glutathione disulfide) or
limited proteolysis, which results in irreversible conversion.
- The conversion can also occur in vivo.
- Formerly EC 220.127.116.11 and EC 18.104.22.168.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
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entries corresponding to 1.17.3.-
entries corresponding to 1.17.-.-
entries corresponding to 1.-.-.-