EC Number | Cloned (Comment) | Organism |
---|---|---|
1.7.2.1 | expression in Escherichia coli | Achromobacter xylosoxidans |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.7.2.1 | 0.035 | - |
NO2- | - |
Achromobacter xylosoxidans |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.7.2.1 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.7.2.1 | Achromobacter xylosoxidans | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.7.2.1 | recombinant enzyme | Achromobacter xylosoxidans |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.7.2.1 | 10.8 | - |
recombinant enzyme, without activation, enzyme has only type 1 copper centers | Achromobacter xylosoxidans |
1.7.2.1 | 167.7 | - |
recombinant enzyme, after activation with CuSO4 | Achromobacter xylosoxidans |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.7.2.1 | nitrite + ferrocytochrome c | - |
Achromobacter xylosoxidans | nitric oxide + H2O + ferricytochrome c | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.7.2.1 | trimer | recombinant enzyme | Achromobacter xylosoxidans |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.7.2.1 | 80 | - |
native and purified enzyme retain 50% activity after 20 min exposure | Achromobacter xylosoxidans |