Crystallization (Comment) | Organism |
---|---|
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method | Arthrobacter globiformis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0025 | - |
2-Phenylethylamine | pH 6.8, 30°C, Co-activated enzyme | Arthrobacter globiformis | |
0.0025 | - |
2-Phenylethylamine | pH 6.8, 30°C, Cu-activated enzyme | Arthrobacter globiformis | |
0.0034 | - |
2-Phenylethylamine | pH 6.8, 30°C, Ni-activated enzyme | Arthrobacter globiformis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ | Arthrobacter globiformis | |
Cu2+ | besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ | Arthrobacter globiformis | |
Ni2+ | besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+ | Arthrobacter globiformis | |
Zn2+ | besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently | Arthrobacter globiformis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arthrobacter globiformis | P46881 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme expressed in Escherichia coli | Arthrobacter globiformis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-phenylethylamine + H2O + O2 | - |
Arthrobacter globiformis | 2-phenylethanal + NH3 + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AGAO | - |
Arthrobacter globiformis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.63 | - |
2-Phenylethylamine | pH 6.8, 30°C, Ni-activated enzyme | Arthrobacter globiformis | |
0.92 | - |
2-Phenylethylamine | pH 6.8, 30°C, Co-activated enzyme | Arthrobacter globiformis | |
75.7 | - |
2-Phenylethylamine | pH 6.8, 30°C, Cu-activated enzyme | Arthrobacter globiformis |