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 (Comment) | Organism |
---|---|
C535A/C992R/C1324S triple mutant XDH crystal structure analysis | Rattus norvegicus |
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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Homo sapiens | 5829 | - |
cytosol | - |
Rattus norvegicus | 5829 | - |
extracellular | - |
Bos taurus | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Gallus gallus | - |
- |
- |
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Rhodobacter capsulatus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
from liver | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
milk | - |
Bos taurus | - |
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 | 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 | 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 | 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 | 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 |