EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | thiol active compounds | reversible conversion of xanthine dehydrogenase to xanthine oxidase by modification of C535 and C992 and formation of a disulfide bond, that induces a conformational change | Bos taurus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.17.1.4 | 2.1 A resolution for both xanthine oxidase and dehydrogenase forms, irreversible pancreatin cleaved xanthine oxidase form results in blocking access of substrate NAD+ to the FAD cofactor | Bos taurus |
1.17.3.2 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | Iron-sulfur-center | 2 Fe2-S2-clusters, located at the N-terminal 20 kDa domain | Bos taurus | |
1.17.1.4 | molybdenum-center | C-terminal 85 kDa molybdopterin-binding domain | Bos taurus | |
1.17.3.2 | Iron | iron-molybdenum protein | Bos taurus | |
1.17.3.2 | Molybdenum | an iron-molybdenum protein | Bos taurus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.17.1.4 | 145000 | - |
2 * 145000, data from crystallization | Bos taurus |
1.17.1.4 | 290000 | - |
- |
Bos taurus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | hypoxanthine + NAD+ + H2O | Bos taurus | - |
xanthine + NADH + H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | Bos taurus | - |
urate + NADH | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.1.4 | Bos taurus | - |
- |
- |
1.17.3.2 | Bos taurus | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.17.3.2 | 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 |
1.17.3.2 | proteolytic modification | - |
Bos taurus |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.17.1.4 | - |
Bos taurus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.17.1.4 | milk | - |
Bos taurus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Bos taurus | xanthine + NADH + H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | - |
Bos taurus | urate + NADH | - |
? | |
1.17.3.2 | hypoxanthine + 2 H2O + 2 O2 | - |
Bos taurus | urate + 2 H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | electron acceptor O2 | Bos taurus | uric acid + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.17.1.4 | dimer | 2 * 145000, data from crystallization | Bos taurus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | FAD | one FAD per subunit, central 40 kDa FAD-domain | Bos taurus | |
1.17.1.4 | additional information | - |
Bos taurus | |
1.17.1.4 | NAD+ | - |
Bos taurus | |
1.17.3.2 | FAD | flavoprotein | Bos taurus | |
1.17.3.2 | 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 |