Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Achromobacter xylosoxidans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.035 | - |
NO2- | - |
Achromobacter xylosoxidans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | blue copper enzyme that shows little absorbance in the 460 nm range, purified recombinant nonactivated enzyme contains 1.97 mol Copper/mol enzyme, the CuSO4 activated enzyme contains 5.97 mol copper/mol enzyme i.e. 6 copper atoms per trimer, CuSO4 activation restores type 2 copper centers which are the sites of catalysis | Achromobacter xylosoxidans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Achromobacter xylosoxidans | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Achromobacter xylosoxidans |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
10.8 | - |
recombinant enzyme, without activation, enzyme has only type 1 copper centers | Achromobacter xylosoxidans |
167.7 | - |
recombinant enzyme, after activation with CuSO4 | Achromobacter xylosoxidans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + ferrocytochrome c | - |
Achromobacter xylosoxidans | nitric oxide + H2O + ferricytochrome c | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | recombinant enzyme | Achromobacter xylosoxidans |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
native and purified enzyme retain 50% activity after 20 min exposure | Achromobacter xylosoxidans |