EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.4.3.21 | holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method | Arthrobacter globiformis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.21 | 0.0025 | - |
2-Phenylethylamine | pH 6.8, 30°C, Co-activated enzyme | Arthrobacter globiformis | |
1.4.3.21 | 0.0025 | - |
2-Phenylethylamine | pH 6.8, 30°C, Cu-activated enzyme | Arthrobacter globiformis | |
1.4.3.21 | 0.0034 | - |
2-Phenylethylamine | pH 6.8, 30°C, Ni-activated enzyme | Arthrobacter globiformis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.21 | 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 | |
1.4.3.21 | 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 | |
1.4.3.21 | 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 | |
1.4.3.21 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.21 | Arthrobacter globiformis | P46881 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.4.3.21 | recombinant enzyme expressed in Escherichia coli | Arthrobacter globiformis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.21 | 2-phenylethylamine + H2O + O2 | - |
Arthrobacter globiformis | 2-phenylethanal + NH3 + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.21 | AGAO | - |
Arthrobacter globiformis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.21 | 0.63 | - |
2-Phenylethylamine | pH 6.8, 30°C, Ni-activated enzyme | Arthrobacter globiformis | |
1.4.3.21 | 0.92 | - |
2-Phenylethylamine | pH 6.8, 30°C, Co-activated enzyme | Arthrobacter globiformis | |
1.4.3.21 | 75.7 | - |
2-Phenylethylamine | pH 6.8, 30°C, Cu-activated enzyme | Arthrobacter globiformis |