Cloned (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
D79A | the KM-value for urate is 82% of the wild-type value | Bacillus subtilis |
K9M | mutant enzyme has a maximal velocity of 0.4% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 1.5fold higher than that of the wild-type enzyme | Bacillus subtilis |
T69A | mutant enzyme has a maximal velocity of 3% of the wild-type value. Ionization at pH 6.4 that is observed with the wild-type enzyme is absent in the mutant. The KM-value for urate is 5fold higher than that of the wild-type enzyme | Bacillus subtilis |
T69A/K9M | the KM-value for urate is 16.1fold higher than that of the wild-type enzyme | Bacillus subtilis |
T69V | the KM-value for urate is 30.9fold higher than that of the wild-type enzyme | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.028 | - |
Urate | pH 8.0, mutant enzyme D70A | Bacillus subtilis | |
0.034 | - |
Urate | pH 8.0, wild-type enzyme | Bacillus subtilis | |
0.051 | - |
Urate | pH 8.0, mutant enzyme K9M | Bacillus subtilis | |
0.17 | - |
Urate | pH 8.0, mutant enzyme T69A | Bacillus subtilis | |
0.547 | - |
Urate | pH 8.0, mutant enzyme T69A/K9M | Bacillus subtilis | |
1.05 | - |
Urate | pH 8.0, mutant enzyme T69V | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
urate + O2 + H2O | it is proposed that T69 and K9 form a catalytic diad in which K9 deprotonates T69 to allow it to abstract the proton from the N9 position of the substrate to generate the dianion | Bacillus subtilis | 5-hydroxyisourate + H2O2 | - |
? |