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Information on EC 1.17.1.4 - xanthine dehydrogenase

for references in articles please use BRENDA:EC1.17.1.4

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IUBMB Comments

Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein . The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].

The enzyme appears in viruses and cellular organisms

Synonyms
xdh/xo, xanthine dehydrogenase/oxidase, atxdh1, paoabc, xanthine:nad+ oxidoreductase, xanthine dehydrogenase-1, xanthine-nad oxidoreductase, xanthine/nad+ oxidoreductase, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthine + NAD+ + H2O = urate + NADH + H+
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
MetaCyc
adenosine nucleotides degradation I, adenosine nucleotides degradation II, caffeine degradation III (bacteria, via demethylation), guanosine nucleotides degradation I, guanosine nucleotides degradation II, guanosine nucleotides degradation III, inosine 5'-phosphate degradation, purine nucleobases degradation II (anaerobic), theophylline degradation