Crystallization (Comment) | Organism |
---|---|
2.5 A resolution, each enzyme subunit is composed of an N-terminal 20000 Da domain containing two iron sulfur centers, a central 40000 Da FAD domain and a C-terminal 85000 molybdopterin binding domain, the four redox centers are aligned in a linear fashion | Bos taurus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | iron-molybdenum protein | Bos taurus | |
Molybdenum | an iron-molybdenum protein | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | reversible conversion of xanthine dehydrogenase to xanthin oxidase can be achieved by modification of Cys535 and Cys992, tryptic proteolysis of xanthine dehydrogenase after Lys551 or pancreatin cleavage after Leu219 and Lys569 results in irreversible transformation to xanthine oxidase | Bos taurus |
proteolytic modification | - |
Bos taurus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hypoxanthine + 2 H2O + 2 O2 | - |
Bos taurus | urate + 2 H2O2 | - |
? | |
xanthine + H2O + O2 | electron acceptor O2 | Bos taurus | uric acid + H2O2 | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoprotein | Bos taurus | |
molybdopterin | one cofactor per subunit, oxidation of xanthine takes place at this center, electrons are rapidly distributed to the other centers by intramolecular electron transfer | Bos taurus |