ENZYME entry: EC 1.17.1.4

Accepted Name

xanthine dehydrogenase

Alternative Name(s)

NAD-xanthine dehydrogenase

xanthine/NAD(+) oxidoreductase

xanthine-NAD oxidoreductase

xanthine oxidoreductase

Reaction catalysed

H2O + NAD(+) + xanthine <=> H(+) + NADH + urate

Comment(s)

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 center.
The mammallian 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, EC 1.17.3.2.
The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion.
The conversion can also occur in vivo.
Formerly EC 1.1.1.204 and EC 1.2.1.37.

Cross-references

BRENDA

EC2PDB

ExplorEnz

PRIAM enzyme-specific profiles

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

IntEnz

MEDLINE

MetaCyc

Rhea expert-curated reactions

UniProtKB/Swiss-Prot

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.

All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.17.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.17.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-