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Literature summary for 1.17.1.4 extracted from
- Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase (2008), FEBS J., 275, 3278-3289.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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)
| Crystallization (Comment) | Organism |
|---|---|
| C535A/C992R/C1324S triple mutant XDH crystal structure analysis | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C535A/C992R/C1324S | an XDH-locked enzyme mutant that cannot be induced by sulfhydryl reagents to adopt the XO form | Rattus norvegicus |
| 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 |
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 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
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Homo sapiens | 5829 | - |
| cytosol | - |
Rattus norvegicus | 5829 | - |
| extracellular | - |
Bos taurus | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hypoxanthine + NAD+ + H2O | Gallus gallus | - |
xanthine + NADH + H+ | - |
? |  |
| hypoxanthine + NAD+ + H2O | Homo sapiens | - |
xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | Rattus norvegicus | - |
xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | Bos taurus | - |
xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
xanthine + NADH + H+ | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| xanthine + NAD+ + H2O | Gallus gallus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Homo sapiens | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Rattus norvegicus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Bos taurus | - |
urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | Rhodobacter capsulatus | - |
urate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
| Gallus gallus | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Rhodobacter capsulatus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| from liver | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Homo sapiens | - |
| liver | - |
Rattus norvegicus | - |
| milk | - |
Bos taurus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hypoxanthine + NAD+ + H2O | - |
Gallus gallus | xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | - |
Homo sapiens | xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | - |
Rattus norvegicus | xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | - |
Bos taurus | xanthine + NADH + H+ | - |
? | |
| hypoxanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | xanthine + NADH + H+ | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| xanthine + NAD+ + H2O | - |
Gallus gallus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Homo sapiens | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Rattus norvegicus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Bos taurus | urate + NADH + H+ | - |
? | |
| xanthine + NAD+ + H2O | - |
Rhodobacter capsulatus | urate + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Gallus gallus |
| More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Homo sapiens |
| More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Rattus norvegicus |
| More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Bos taurus |
| More | structural comparison of xanthine dehydrogenase and xanthine oxidase, EC 1.17.3.2, overview | Rhodobacter capsulatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| xanthine oxidoreductase | - |
Gallus gallus |
| xanthine oxidoreductase | - |
Homo sapiens |
| xanthine oxidoreductase | - |
Rattus norvegicus |
| xanthine oxidoreductase | - |
Bos taurus |
| xanthine oxidoreductase | - |
Rhodobacter capsulatus |
| XDH | - |
Gallus gallus |
| XDH | - |
Homo sapiens |
| XDH | - |
Rattus norvegicus |
| XDH | - |
Bos taurus |
| XDH | - |
Rhodobacter capsulatus |
| XOR | - |
Gallus gallus |
| XOR | - |
Homo sapiens |
| XOR | - |
Rattus norvegicus |
| XOR | - |
Bos taurus |
| XOR | - |
Rhodobacter capsulatus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Homo sapiens | |
| FAD | - |
Bos taurus | |
| FAD | the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview | Rattus norvegicus | |
| molybdenum cofactor | structure-function analysis, mechanism, overview | Gallus gallus | |
| molybdenum cofactor | structure-function analysis, mechanism, overview | Homo sapiens | |
| molybdenum cofactor | structure-function analysis, mechanism, overview | Rattus norvegicus | |
| molybdenum cofactor | structure-function analysis, mechanism, overview | Bos taurus | |
| molybdenum cofactor | structure-function analysis, mechanism, overview | Rhodobacter capsulatus | |
| NAD+ | - |
Gallus gallus | |
| NAD+ | - |
Homo sapiens | |
| NAD+ | - |
Rattus norvegicus | |
| NAD+ | - |
Bos taurus | |
| NAD+ | - |
Rhodobacter capsulatus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
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