EC Number | Cloned (Comment) | Organism |
---|---|---|
1.17.1.4 | expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form | Rattus norvegicus |
1.17.3.2 | expression of enzyme mutant D428A in Spodoptera frugiperda Sf9 cells via the baculovirus transfection system in mostly the demolybdo-form | Rattus norvegicus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.17.1.4 | highly active bovine XOR in its XDH form is soaked in a large excess of NADH under strictly anaerobic conditions in order to reduce both FAD cofactor and iron sulfur centers and to block any electron transfer from the Mo center. The Mo ions in the crystal are fully reduced by soaking in 4 mM titanium citrate solution followed by 0.25 mM urate, crystal structure determination and analysis, superimposition, modelling | Bos taurus |
1.17.1.4 | XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution | Rattus norvegicus |
1.17.3.2 | urate complexes of the reduced form of native milk enzyme reaction intermediate, X-ray diffraction structure determination and analysis at 2.1 A resolution | Bos taurus |
1.17.3.2 | XOR complexed with the artificial substrate 4-[5-pyridine-4-yl-1H-[1,2,4]triazol-3-yl]pyridine-2-carbonitril, FYX-051, crystal structure analysis. Urate complexes of the purified recombinant demolybdo-form of mutant D428A, X-ray diffraction structure determination and analysis at 1.7 A resolution | Rattus norvegicus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.17.3.2 | extracellular | - |
Bos taurus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | Iron | two [2Fe-2S] centers | Bos taurus | |
1.17.1.4 | Iron | two [2Fe-2S] centers | Rattus norvegicus | |
1.17.1.4 | Molybdenum | XOR is a molybdenum-containing enzyme, cofactor geometry, overview | Bos taurus | |
1.17.1.4 | Molybdenum | XOR is a molybdenum-containing enzyme, cofactor geometry, overview | Rattus norvegicus | |
1.17.3.2 | Iron | two [2Fe-2S] centers | Bos taurus | |
1.17.3.2 | Iron | two [2Fe-2S] centers | Rattus norvegicus | |
1.17.3.2 | Molybdenum | XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions, in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview | Rattus norvegicus | |
1.17.3.2 | Molybdenum | XOR is a molybdenum-containing enzyme. In the oxidized form of XORs, the Mo(VI) ion is in the center of a square-pyramidal geometry, coordinated by an oxo-ligand at the apical position and one hydroxo and one sulfido ligand at equatorial positions,3a in addition to the two vicinal sulfur ligands contributed by the pterin group, cofactor geometry, overview | Bos taurus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | hypoxanthine + 2 NAD+ + 2 H2O | Bos taurus | - |
urate + 2 NADH + 2 H+ | - |
? | |
1.17.1.4 | hypoxanthine + 2 NAD+ + 2 H2O | Rattus norvegicus | - |
urate + 2 NADH + 2 H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | Bos taurus | catalytically relevant binding mode of the substrate xanthine, overview | urate + NADH + H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | Rattus norvegicus | catalytically relevant binding mode of the substrate xanthine, overview | urate + NADH + H+ | - |
? | |
1.17.3.2 | hypoxanthine + 2 H2O + 2 O2 | Bos taurus | - |
urate + 2 H2O2 | - |
? | |
1.17.3.2 | hypoxanthine + 2 H2O + 2 O2 | Rattus norvegicus | - |
urate + 2 H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | Bos taurus | catalytically relevant binding mode of the substrate xanthine, overview | urate + H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | Rattus norvegicus | catalytically relevant binding mode of the substrate xanthine, overview | urate + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.1.4 | Bos taurus | - |
- |
- |
1.17.1.4 | Rattus norvegicus | P22985 | cf. EC 1.17.3.2 | - |
1.17.3.2 | Bos taurus | - |
- |
- |
1.17.3.2 | Rattus norvegicus | P22985 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.17.1.4 | highly active bovine XOR in its XDH form is prepared by folate affinity chromatography | Bos taurus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.17.1.4 | xanthine + NAD+ + H2O = urate + NADH + H+ | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Bos taurus | |
1.17.1.4 | xanthine + NAD+ + H2O = urate + NADH + H+ | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Rattus norvegicus | |
1.17.3.2 | xanthine + H2O + O2 = urate + H2O2 | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Bos taurus | |
1.17.3.2 | xanthine + H2O + O2 = urate + H2O2 | reaction mechanism of XOR and binding modes of the substrate xanthine, overview. The oxidative hydroxylation of purine substrates takes place at the molybdenum center. Reducing equivalents introduced there are then transferred via two [2Fe-2S] centers to the FAD cofactor where reduction of the physiological electron acceptors occurs, NAD+ in the case of the dehydrogenase form, XDH, or O2 in the oxidase form, XO, of the enzyme occur | Rattus norvegicus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.17.1.4 | milk | - |
Bos taurus | - |
1.17.3.2 | milk | - |
Bos taurus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.1.4 | hypoxanthine + 2 NAD+ + 2 H2O | - |
Bos taurus | urate + 2 NADH + 2 H+ | - |
? | |
1.17.1.4 | hypoxanthine + 2 NAD+ + 2 H2O | - |
Rattus norvegicus | urate + 2 NADH + 2 H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | catalytically relevant binding mode of the substrate xanthine, overview | Bos taurus | urate + NADH + H+ | - |
? | |
1.17.1.4 | xanthine + NAD+ + H2O | catalytically relevant binding mode of the substrate xanthine, overview | Rattus norvegicus | urate + NADH + H+ | - |
? | |
1.17.3.2 | hypoxanthine + 2 H2O + 2 O2 | - |
Bos taurus | urate + 2 H2O2 | - |
? | |
1.17.3.2 | hypoxanthine + 2 H2O + 2 O2 | - |
Rattus norvegicus | urate + 2 H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | catalytically relevant binding mode of the substrate xanthine, overview | Bos taurus | urate + H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | catalytically relevant binding mode of the substrate xanthine, overview | Rattus norvegicus | urate + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.17.1.4 | More | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |
1.17.1.4 | More | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
1.17.1.4 | XDH | - |
Bos taurus |
1.17.1.4 | XDH | - |
Rattus norvegicus |
1.17.1.4 | XOR | - |
Bos taurus |
1.17.1.4 | XOR | - |
Rattus norvegicus |
1.17.3.2 | More | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
1.17.3.2 | More | XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |
1.17.3.2 | xanthine oxidoreductase | - |
Bos taurus |
1.17.3.2 | xanthine oxidoreductase | - |
Rattus norvegicus |
1.17.3.2 | XOR | - |
Bos taurus |
1.17.3.2 | XOR | - |
Rattus norvegicus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | FAD | - |
Bos taurus | |
1.17.1.4 | FAD | role of Asp428 in the FAD reactivity, overview | Rattus norvegicus | |
1.17.1.4 | molybdenum cofactor | cofactor geometry, overview | Bos taurus | |
1.17.1.4 | molybdopterin | cofactor geometry, overview | Rattus norvegicus | |
1.17.1.4 | additional information | cofactor conformation, binding structure analysis and mechanism, overview | Bos taurus | |
1.17.1.4 | additional information | cofactor conformation, binding structure analysis and mechanism, overview | Rattus norvegicus | |
1.17.1.4 | NAD+ | - |
Bos taurus | |
1.17.1.4 | NAD+ | - |
Rattus norvegicus | |
1.17.3.2 | FAD | - |
Bos taurus | |
1.17.3.2 | FAD | role of Asp428 in the FAD reactivity, overview | Rattus norvegicus | |
1.17.3.2 | molybdenum cofactor | cofactor geometry, overview | Bos taurus | |
1.17.3.2 | molybdenum cofactor | cofactor geometry, overview | Rattus norvegicus | |
1.17.3.2 | additional information | cofactor conformation, binding structure analysis and mechanism, overview | Bos taurus | |
1.17.3.2 | additional information | cofactor conformation, binding structure analysis and mechanism, overview | Rattus norvegicus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.17.1.4 | additional information | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |
1.17.1.4 | additional information | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
1.17.3.2 | additional information | XOR can adopt its XOR xanthine oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Rattus norvegicus |
1.17.3.2 | additional information | XOR can adopt its XOR xanthone oxidoreductase form EC 1.17.3.2, and its xanthine dehydrogenase form, XDH, EC 1.17.1.4 | Bos taurus |