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Literature summary extracted from
- Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase (2008), FEBS J., 275, 3278-3289.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.1.4 | additional information | activation mechanism based on the results of mutations at the positions of the second Glu and Arg residues, overview | Rhodobacter capsulatus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.17.1.4 | C535A/C992R/C1324S triple mutant XDH crystal structure analysis | Rattus norvegicus |
| 1.17.3.2 | W335A/F336L double mutant enzyme crystal structure analysis | Rattus norvegicus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | C535A/C992R/C1324S | an XDH-locked enzyme mutant that cannot be induced by sulfhydryl reagents to adopt the XO form | Rattus norvegicus |
| 1.17.1.4 | E803V | very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction | Homo sapiens |
| 1.17.1.4 | R881M | very low steady-state activity towards xanthine or hypoxanthine, loss of hydrogen bonding with one of these residues greatly influences the electron transfer process to the molybdenum center, changing the rate-limiting step in the reductive half-reaction | Homo sapiens |
| 1.17.3.2 | W335A/F336L | xanthine oxidase locked mutant | Rattus norvegicus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.17.1.4 | additional information | - |
additional information | 2-position hydroxylation is crucial for 8-position hydroxylation. Stopped-flow studies indicate that the rate-limiting step of the reductive half-reaction is not electron transfer from the xanthine substrate to the molybdenum center, but product release | Rhodobacter capsulatus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.17.1.4 | cytosol | - |
Homo sapiens | 5829 | - |
| 1.17.1.4 | cytosol | - |
Rattus norvegicus | 5829 | - |
| 1.17.1.4 | extracellular | - |
Bos taurus | - |
- |
| 1.17.3.2 | cytosol | - |
Rattus norvegicus | 5829 | - |
| 1.17.3.2 | extracellular | secreted to milk | Bos taurus | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | Gallus gallus | - |
xanthine + NADH + H+ | - |
? |  |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | Homo sapiens | - |
xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | Rattus norvegicus | - |
xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | Bos taurus | - |
xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | additional information | Rattus norvegicus | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. The difference in three-dimensional structures is centered on Ala535. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | ? | - |
? | |
| 1.17.1.4 | additional information | Gallus gallus | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | ? | - |
? | |
| 1.17.1.4 | additional information | Homo sapiens | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | ? | - |
? | |
| 1.17.1.4 | additional information | Bos taurus | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | ? | - |
? | |
| 1.17.1.4 | additional information | Rhodobacter capsulatus | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | ? | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | Gallus gallus | - |
urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | Homo sapiens | - |
urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | Rattus norvegicus | - |
urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | Bos taurus | - |
urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
urate + NADH + H+ | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | Rattus norvegicus | - |
urate + H2O2 | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | Bos taurus | - |
urate + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.1.4 | Bos taurus | - |
- |
- |
| 1.17.1.4 | Gallus gallus | - |
- |
- |
| 1.17.1.4 | Homo sapiens | - |
- |
- |
| 1.17.1.4 | Rattus norvegicus | - |
- |
- |
| 1.17.1.4 | Rhodobacter capsulatus | - |
- |
- |
| 1.17.3.2 | Bos taurus | - |
- |
- |
| 1.17.3.2 | Rattus norvegicus | - |
male Wistar rats | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.17.1.4 | from liver | Rattus norvegicus |
| 1.17.3.2 | from liver | Rattus norvegicus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.17.1.4 | liver | - |
Homo sapiens | - |
| 1.17.1.4 | liver | - |
Rattus norvegicus | - |
| 1.17.1.4 | milk | - |
Bos taurus | - |
| 1.17.3.2 | liver | - |
Rattus norvegicus | - |
| 1.17.3.2 | milk | - |
Bos taurus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Gallus gallus | xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Homo sapiens | xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Rattus norvegicus | xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Bos taurus | xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | hypoxanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | xanthine + NADH + H+ | - |
? | |
| 1.17.1.4 | additional information | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. The difference in three-dimensional structures is centered on Ala535. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | Rattus norvegicus | ? | - |
? | |
| 1.17.1.4 | additional information | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | Gallus gallus | ? | - |
? | |
| 1.17.1.4 | additional information | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | Homo sapiens | ? | - |
? | |
| 1.17.1.4 | additional information | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | Bos taurus | ? | - |
? | |
| 1.17.1.4 | additional information | xanthine dehydrogenase, XDH, can be converted to xanthine oxidase, XO, by a highly sophisticated mechanism, overview. The transition seems to involve a thermodynamic equilibrium between XDH and XO, disulfide bond formation or proteolysis can then lock the enzyme in the XO form. XDH and XO forms are in a thermodynamic equilibrium with a relatively low energy barrier between the two forms | Rhodobacter capsulatus | ? | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | - |
Gallus gallus | urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | - |
Homo sapiens | urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | - |
Rattus norvegicus | urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | - |
Bos taurus | urate + NADH + H+ | - |
? | |
| 1.17.1.4 | xanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | urate + NADH + H+ | - |
? | |
| 1.17.3.2 | FYX-051 + O2 + H2O | the structure of bovine XOR exposed to the slow-reacting substrate FYX-051 shows a covalent intermediate of the hydroxylation reaction, in which the hydroxyl oxygen bridged the molybdenumatom and the acceptor carbon atom of the aromatic ring of the substrate | Bos taurus | ? | - |
? | |
| 1.17.3.2 | additional information | the oxidation of xanthine takes place at the molybdenum center, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group | Bos taurus | ? | - |
? | |
| 1.17.3.2 | additional information | the oxidation of xanthine takes place at the molybdenum cofactor, and the electrons thus introduced are rapidly transferred to FAD via the Fe-SI and Fe-SII centers. Glu1261, located near the Mo-OH in the salicylate bound-form of XOR, initiates catalysis by deprotonating the Mo-OH group | Rattus norvegicus | ? | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | - |
Rattus norvegicus | urate + H2O2 | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | - |
Bos taurus | urate + H2O2 | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | binding modes of the substrate xanthine and mechanism of its hydroxylation, overview | Rattus norvegicus | urate + H2O2 | - |
? | |
| 1.17.3.2 | xanthine + O2 + H2O | binding modes of the substrate xanthine and mechanism of its hydroxylation, overview | Bos taurus | urate + H2O2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Gallus gallus |
| 1.17.1.4 | More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Homo sapiens |
| 1.17.1.4 | More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Rattus norvegicus |
| 1.17.1.4 | More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Bos taurus |
| 1.17.1.4 | More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Rhodobacter capsulatus |
| 1.17.3.2 | More | structural comparison of xanthine dehydrogenase, EC 1.17.1.4, and xanthine oxidase, overview | Rattus norvegicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | xanthine oxidoreductase | - |
Gallus gallus |
| 1.17.1.4 | xanthine oxidoreductase | - |
Homo sapiens |
| 1.17.1.4 | xanthine oxidoreductase | - |
Rattus norvegicus |
| 1.17.1.4 | xanthine oxidoreductase | - |
Bos taurus |
| 1.17.1.4 | xanthine oxidoreductase | - |
Rhodobacter capsulatus |
| 1.17.1.4 | XDH | - |
Gallus gallus |
| 1.17.1.4 | XDH | - |
Homo sapiens |
| 1.17.1.4 | XDH | - |
Rattus norvegicus |
| 1.17.1.4 | XDH | - |
Bos taurus |
| 1.17.1.4 | XDH | - |
Rhodobacter capsulatus |
| 1.17.1.4 | XOR | - |
Gallus gallus |
| 1.17.1.4 | XOR | - |
Homo sapiens |
| 1.17.1.4 | XOR | - |
Rattus norvegicus |
| 1.17.1.4 | XOR | - |
Bos taurus |
| 1.17.1.4 | XOR | - |
Rhodobacter capsulatus |
| 1.17.3.2 | xanthine oxidoreductase | - |
Rattus norvegicus |
| 1.17.3.2 | xanthine oxidoreductase | - |
Bos taurus |
| 1.17.3.2 | XOR | - |
Rattus norvegicus |
| 1.17.3.2 | XOR | - |
Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.1.4 | FAD | - |
Homo sapiens | |
| 1.17.1.4 | FAD | - |
Bos taurus | |
| 1.17.1.4 | FAD | the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview | Rattus norvegicus | |
| 1.17.1.4 | molybdenum cofactor | structure-function analysis, mechanism, overview | Gallus gallus | |
| 1.17.1.4 | molybdenum cofactor | structure-function analysis, mechanism, overview | Homo sapiens | |
| 1.17.1.4 | molybdenum cofactor | structure-function analysis, mechanism, overview | Rattus norvegicus | |
| 1.17.1.4 | molybdenum cofactor | structure-function analysis, mechanism, overview | Bos taurus | |
| 1.17.1.4 | molybdenum cofactor | structure-function analysis, mechanism, overview | Rhodobacter capsulatus | |
| 1.17.1.4 | NAD+ | - |
Gallus gallus | |
| 1.17.1.4 | NAD+ | - |
Homo sapiens | |
| 1.17.1.4 | NAD+ | - |
Rattus norvegicus | |
| 1.17.1.4 | NAD+ | - |
Bos taurus | |
| 1.17.1.4 | NAD+ | - |
Rhodobacter capsulatus | |
| 1.17.3.2 | FAD | the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview | Rattus norvegicus | |
| 1.17.3.2 | FAD | the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview | Bos taurus | |
| 1.17.3.2 | molybdenum cofactor | structure-function analysis, mechanism, overview | Rattus norvegicus | |
| 1.17.3.2 | molybdenum cofactor | structure-function analysis, mechanism, overview | Bos taurus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.17.1.4 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Gallus gallus |
| 1.17.1.4 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Homo sapiens |
| 1.17.1.4 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Rattus norvegicus |
| 1.17.1.4 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Bos taurus |
| 1.17.1.4 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Rhodobacter capsulatus |
| 1.17.3.2 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Rattus norvegicus |
| 1.17.3.2 | physiological function | xanthine oxidoreductase catalyzes the oxidation of hypoxanthine to xanthine or xanthine to uric acid in the metabolic pathway of purine degradation | Bos taurus |
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