EC Number | Cloned (Comment) | Organism |
---|---|---|
1.4.3.21 | expressed in Escherichia coli JM109 cells | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.21 | EDTA | treatment with EDTA reduces the activity of wild type enzyme | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.21 | 0.0012 | - |
2-Phenylethylamine | wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.21 | Ca2+ | calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity | Escherichia coli | |
1.4.3.21 | Cu2+ | the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal | Escherichia coli | |
1.4.3.21 | Mg2+ | enzyme activity is stimulated by 3 mM | Escherichia coli | |
1.4.3.21 | Mn2+ | enzyme activity is stimulated by 3 mM | Escherichia coli | |
1.4.3.21 | additional information | not activated by Zn2+ | Escherichia coli | |
1.4.3.21 | Sr2+ | enzyme activity is stimulated by 3 mM | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.21 | RCH2NH2 + H2O + O2 | Escherichia coli | - |
RCHO + NH3 + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.21 | Escherichia coli | P46883 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.4.3.21 | Q-Sepharose column chromatography, and gel filtration | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.21 | 2-phenylethylamine + H2O + O2 | - |
Escherichia coli | 2-phenylethanal + NH3 + H2O2 | - |
? | |
1.4.3.21 | RCH2NH2 + H2O + O2 | - |
Escherichia coli | RCHO + NH3 + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.4.3.21 | homodimer | x-ray crystallography | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.21 | Copper amine oxidase | - |
Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.21 | 12.4 | - |
2-Phenylethylamine | wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.21 | 2,4,5-trihydroxyphenylalanine quinone | - |
Escherichia coli |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.3.21 | 10330 | - |
2-Phenylethylamine | wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C | Escherichia coli |