Inhibitors | Comment | Organism | Structure |
---|---|---|---|
azide | - |
Sus scrofa | |
cyanide | uncompetitive vs. benzylamine, non-competititve vs. O2 | Sus scrofa | |
NaN3 | azide binds to Cu2+ ions, competitive inhibition vs. O2, uncompetitive vs. benzylamine | Sus scrofa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions | Sus scrofa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
97000 | - |
2 * 97000, SDS-PAGE | Sus scrofa |
186000 | - |
sedimentation-equilibrium | Sus scrofa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
blood plasma | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
RCH2NH2 + H2O + O2 | - |
Sus scrofa | RCHO + NH3 + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 97000, SDS-PAGE | Sus scrofa |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.76 | - |
cyanide | vs. O2, deduced from slope | Sus scrofa | |
2.17 | - |
cyanide | vs. benzylamine | Sus scrofa | |
2.9 | - |
cyanide | vs. O2, deduced from intercept | Sus scrofa | |
40 | - |
azide | vs. benzylamine | Sus scrofa | |
84 | - |
azide | vs. O2 | Sus scrofa |