Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sharma, N.K.; Thakur, S.; Thakur, N.; Savitri, N.; Bhalla, T.C.
    Thermostable xanthine oxidase activity from Bacillus pumilus RL-2d isolated from Manikaran thermal spring production and characterization (2016), Indian J. Microbiol., 56, 88-98 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.3.2 gene xdh, DNA and amino acid sequence determination and analysis Bacillus pumilus

Inhibitors

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-

Reaction

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

Source Tissue

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
-

Substrates and Products (Substrate)

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
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.3.2 75
-
assay at Bacillus pumilus

Temperature Stability [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.3.2 7.6
-
assay at Bacillus pumilus

Cofactor

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

General Information

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