EC Number | Cloned (Comment) | Organism |
---|---|---|
1.17.3.2 | gene xdh, DNA and amino acid sequence determination and analysis | Bacillus pumilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.17.3.2 | Ag+ | 85% inhibition at 1 mM | Bacillus pumilus | |
1.17.3.2 | allopurinol | 96% inhibition at 1 mM | Bacillus pumilus | |
1.17.3.2 | Ca2+ | 83% inhibition at 1 mM | Bacillus pumilus | |
1.17.3.2 | Cu2+ | 76% inhibition at 1 mM | Bacillus pumilus | |
1.17.3.2 | DTT | slight inhibition | Bacillus pumilus | |
1.17.3.2 | EDTA | slight inhibition | Bacillus pumilus | |
1.17.3.2 | Hg2+ | 95% inhibition at 1 mM | Bacillus pumilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.3.2 | hypoxanthine + NAD+ + H2O | Bacillus pumilus | - |
xanthine + NADH + H+ | - |
? | |
1.17.3.2 | hypoxanthine + NAD+ + H2O | Bacillus pumilus RL-2d | - |
xanthine + NADH + H+ | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | Bacillus pumilus | - |
urate + H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | Bacillus pumilus RL-2d | - |
urate + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.3.2 | Bacillus pumilus | - |
isolated from soil sample from Manikaran hot spring, India | - |
1.17.3.2 | Bacillus pumilus RL-2d | - |
isolated from soil sample from Manikaran hot spring, India | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.17.3.2 | xanthine + H2O + O2 = urate + H2O2 | the catalytic reaction of xanthine oxidase is initiated by abstraction of a proton from the Mo-OH group by a conserved active site glutamate residue. The oxidative hydroxylation of xanthine to uric acid takes place at the molybdenum center and results in the two-electron reduction of the metal from Mo(VI) to Mo(IV). The enzyme is subsequently re-oxidized by NAD+ or molecular oxygen in a reaction that occurs at the FAD cofactor | Bacillus pumilus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.17.3.2 | cell culture | optimization of culture and growth conditions for Bacillus pumilus strain RL-2d, identified from screening as a strain with hyperactive xanthine oxidase. Medium M6 (pH 7.5, 55°C) containing (g/l) 10.0 g glucose, 3.0 g yeast extract, 1.0 g beef extract, 5.0 g peptone, 5.0 g sodium chloride and 0.152 g xanthine proves to be the best for the xanthine oxidase activity, overview | Bacillus pumilus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.17.3.2 | hypoxanthine + NAD+ + H2O | - |
Bacillus pumilus | xanthine + NADH + H+ | - |
? | |
1.17.3.2 | hypoxanthine + NAD+ + H2O | - |
Bacillus pumilus RL-2d | xanthine + NADH + H+ | - |
? | |
1.17.3.2 | additional information | the catalytic reaction of xanthine oxidase is initiated by abstraction of a proton from the Mo-OH group by a conserved active site glutamate residue. The oxidative hydroxylation of xanthine to uric acid takes place at the molybdenum center and results in the two-electron reduction of the metal from Mo(VI) to Mo(IV). The enzyme is subsequently re-oxidized by NAD+ or molecular oxygen in a reaction that occurs at the FAD cofactor | Bacillus pumilus | ? | - |
? | |
1.17.3.2 | additional information | the catalytic reaction of xanthine oxidase is initiated by abstraction of a proton from the Mo-OH group by a conserved active site glutamate residue. The oxidative hydroxylation of xanthine to uric acid takes place at the molybdenum center and results in the two-electron reduction of the metal from Mo(VI) to Mo(IV). The enzyme is subsequently re-oxidized by NAD+ or molecular oxygen in a reaction that occurs at the FAD cofactor | Bacillus pumilus RL-2d | ? | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | - |
Bacillus pumilus | urate + H2O2 | - |
? | |
1.17.3.2 | xanthine + H2O + O2 | - |
Bacillus pumilus RL-2d | urate + H2O2 | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.17.3.2 | 75 | - |
assay at | Bacillus pumilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.17.3.2 | 40 | - |
t1/2 is 20 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
1.17.3.2 | 50 | - |
t1/2 is 15 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
1.17.3.2 | 50 | 70 | xanthine oxidase of Bacillus pumilus strain RL-2d is quite stable at | Bacillus pumilus |
1.17.3.2 | 60 | - |
t1/2 is 10 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
1.17.3.2 | 70 | - |
t1/2 is 5.7 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
1.17.3.2 | 80 | - |
t1/2 is 1 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
1.17.3.2 | 90 | - |
t1/2 is 0.8 h, xanthine oxidase of Bacillus pumilus strain RL-2d | Bacillus pumilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.17.3.2 | 7.6 | - |
assay at | Bacillus pumilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.3.2 | FAD | - |
Bacillus pumilus | |
1.17.3.2 | molybdopterin | - |
Bacillus pumilus | |
1.17.3.2 | NAD+ | - |
Bacillus pumilus | |
1.17.3.2 | [2Fe-2S]-center | - |
Bacillus pumilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.17.3.2 | physiological function | xanthine oxidase is an important enzyme of purine metabolism that catalyzes the hydroxylation of hypoxanthine to xanthine and then xanthine to uric acid. Xanthine oxidase is used in the oxidation of purines and related compounds and plays a role in biochemical reactions such as hydroxylation of purines, pterines, aromatic heterocycles, aliphatic and aromatic aldehydes and also in the detoxification or activation of endogenous compounds and xenobiotics | Bacillus pumilus |