BRENDA - Enzyme Database

Thermostable xanthine oxidase activity from Bacillus pumilus RL-2d isolated from Manikaran thermal spring production and characterization

Sharma, N.K.; Thakur, S.; Thakur, N.; Savitri, N.; Bhalla, T.C.; Indian J. Microbiol. 56, 88-98 (2016)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.17.3.2
gene xdh, DNA and amino acid sequence determination and analysis
Bacillus pumilus
Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.17.3.2
hypoxanthine + NAD+ + H2O
Bacillus pumilus
-
xanthine + NADH
-
-
?
1.17.3.2
hypoxanthine + NAD+ + H2O
Bacillus pumilus RL-2d
-
xanthine + NADH
-
-
?
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
Organism
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
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.3.2
hypoxanthine + NAD+ + H2O
-
745064
Bacillus pumilus
xanthine + NADH
-
-
-
?
1.17.3.2
hypoxanthine + NAD+ + H2O
-
745064
Bacillus pumilus RL-2d
xanthine + NADH
-
-
-
?
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
745064
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
745064
Bacillus pumilus RL-2d
?
-
-
-
-
1.17.3.2
xanthine + H2O + O2
-
745064
Bacillus pumilus
urate + H2O2
-
-
-
?
1.17.3.2
xanthine + H2O + O2
-
745064
Bacillus pumilus RL-2d
urate + H2O2
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.17.3.2
75
-
assay at
Bacillus pumilus
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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
70
xanthine oxidase of Bacillus pumilus strain RL-2d is quite stable at
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
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
Commentary
Organism
1.17.3.2
7.6
-
assay at
Bacillus pumilus
Cofactor
EC Number
Cofactor
Commentary
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
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.17.3.2
gene xdh, DNA and amino acid sequence determination and analysis
Bacillus pumilus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.17.3.2
hypoxanthine + NAD+ + H2O
Bacillus pumilus
-
xanthine + NADH
-
-
?
1.17.3.2
hypoxanthine + NAD+ + H2O
Bacillus pumilus RL-2d
-
xanthine + NADH
-
-
?
1.17.3.2
xanthine + H2O + O2
Bacillus pumilus
-
urate + H2O2
-
-
?
1.17.3.2
xanthine + H2O + O2
Bacillus pumilus RL-2d
-
urate + H2O2
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.3.2
hypoxanthine + NAD+ + H2O
-
745064
Bacillus pumilus
xanthine + NADH
-
-
-
?
1.17.3.2
hypoxanthine + NAD+ + H2O
-
745064
Bacillus pumilus RL-2d
xanthine + NADH
-
-
-
?
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
745064
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
745064
Bacillus pumilus RL-2d
?
-
-
-
-
1.17.3.2
xanthine + H2O + O2
-
745064
Bacillus pumilus
urate + H2O2
-
-
-
?
1.17.3.2
xanthine + H2O + O2
-
745064
Bacillus pumilus RL-2d
urate + H2O2
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.17.3.2
75
-
assay at
Bacillus pumilus
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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
70
xanthine oxidase of Bacillus pumilus strain RL-2d is quite stable at
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
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 (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.17.3.2
7.6
-
assay at
Bacillus pumilus
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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