Protein Variants | Comment | Organism |
---|---|---|
M502F | mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability | Bacillus subtilis |
M502L | mutations leads to an increase in the redox potential by approx. 100 mV, decrease in the catalytic efficiency, decrease in thermodynamic stability | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.008 | - |
syringaldazine | mutant enzyme M502F | Bacillus subtilis | |
0.009 | - |
syringaldazine | mutant enzyme M502L | Bacillus subtilis | |
0.01 | - |
syringaldazine | wild-type enzyme | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
spore | coat | Bacillus subtilis | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
syringaldazine + H2O | - |
Bacillus subtilis | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CotA laccase | - |
Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.01 | - |
syringaldazine | mutant enzyme M502F | Bacillus subtilis | |
7.4 | - |
syringaldazine | mutant enzyme M502L | Bacillus subtilis | |
18.4 | - |
syringaldazine | wild-type enzyme | Bacillus subtilis |