CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.90 | Alpha-Beta Complex | |
3.90.1170 | Aldehyde Oxidoreductase; domain 3 | |
3.90.1170.50 | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead |
Domain Context
CATH Clusters
Superfamily | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead |
Functional Family | Xanthine dehydrogenase/oxidase |
Enzyme Information
1.17.1.4 |
Xanthine dehydrogenase.
based on mapping to UniProt P80457
Xanthine + NAD(+) + H(2)O = urate + NADH.
-!- 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 O(2)- 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 1.2.1.37 and EC 1.1.1.204.
|
1.17.3.2 |
Xanthine oxidase.
based on mapping to UniProt P80457
Xanthine + H(2)O + O(2) = urate + H(2)O(2).
-!- Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1. -!- 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 1.17.1.4). -!- During purification the enzyme is largely converted to the O(2)- dependent xanthine oxidase 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 1.1.3.22 and EC 1.2.3.2.
|
UniProtKB Entries (1)
P80457 |
XDH_BOVIN
Bos taurus
Xanthine dehydrogenase/oxidase
|
PDB Structure
PDB | 3SR6 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
X-ray Crystal Structure of Arsenite-Inhibited Xanthine Oxidase: Mu-Sulfido,Mu-Oxo Double Bridge between Molybdenum and Arsenic in the Active Site.
J.Am.Chem.Soc.
|