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Literature summary for 1.17.3.2 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
Search for more literature for 1.17.3.2

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 85% inhibition at 1 mM Bacillus pumilus
allopurinol 96% inhibition at 1 mM Bacillus pumilus
Ca2+ 83% inhibition at 1 mM Bacillus pumilus
Cu2+ 76% inhibition at 1 mM Bacillus pumilus
DTT slight inhibition Bacillus pumilus
EDTA slight inhibition Bacillus pumilus
Hg2+ 95% inhibition at 1 mM Bacillus pumilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxanthine + NAD+ + H2O Bacillus pumilus
-
 xanthine + NADH + H+
-
 ?
hypoxanthine + NAD+ + H2O Bacillus pumilus RL-2d
-
 xanthine + NADH + H+
-
 ?
xanthine + H2O + O2 Bacillus pumilus
-
 urate + H2O2
-
 ?
xanthine + H2O + O2 Bacillus pumilus RL-2d
-
 urate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus pumilus
-
 isolated from soil sample from Manikaran hot spring, India
-
Bacillus pumilus RL-2d
-
 isolated from soil sample from Manikaran hot spring, India
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Source Tissue

Source Tissue Comment Organism Textmining
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxanthine + NAD+ + H2O
-
 Bacillus pumilus xanthine + NADH + H+
-
 ?
hypoxanthine + NAD+ + H2O
-
 Bacillus pumilus RL-2d xanthine + NADH + H+
-
 ?
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 ?
-
 ?
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 ?
-
 ?
xanthine + H2O + O2
-
 Bacillus pumilus urate + H2O2
-
 ?
xanthine + H2O + O2
-
 Bacillus pumilus RL-2d urate + H2O2
-
 ?

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 t1/2 is 20 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus
50
-
 t1/2 is 15 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus
50 70 xanthine oxidase of Bacillus pumilus strain RL-2d is quite stable at Bacillus pumilus
60
-
 t1/2 is 10 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus
70
-
 t1/2 is 5.7 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus
80
-
 t1/2 is 1 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus
90
-
 t1/2 is 0.8 h, xanthine oxidase of Bacillus pumilus strain RL-2d Bacillus pumilus

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Bacillus pumilus
molybdopterin
-
 Bacillus pumilus
NAD+
-
 Bacillus pumilus
[2Fe-2S]-center
-
 Bacillus pumilus

General Information

General Information Comment Organism
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