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