EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.4.9.2 | - |
Pseudomonas putida |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.4.9.2 | 2,4-Dinitrophenylhydrazine | - |
Pseudomonas putida | |
1.4.9.2 | 4-nitrophenylhydrazine | - |
Pseudomonas putida | |
1.4.9.2 | hydroxylamine | - |
Pseudomonas putida | |
1.4.9.2 | Semicarbazide | - |
Pseudomonas putida |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.4.9.2 | 20000 | - |
1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE | Pseudomonas putida |
1.4.9.2 | 40000 | - |
1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE | Pseudomonas putida |
1.4.9.2 | 60000 | - |
1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE | Pseudomonas putida |
1.4.9.2 | 120000 | - |
gel filtration and sedimentation equilibrium analysis | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.9.2 | Pseudomonas putida | P0A182 | catalytic subunit | - |
1.4.9.2 | Pseudomonas putida IFO 15366 | P0A182 | catalytic subunit | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.4.9.2 | 13 | - |
25°C, pH 8.0 | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.9.2 | n-amylamine + H2O + 2 blue protein | - |
Pseudomonas putida | ? + NH3 + 2 blue protein | - |
? | |
1.4.9.2 | n-amylamine + H2O + 2 blue protein | - |
Pseudomonas putida IFO 15366 | ? + NH3 + 2 blue protein | - |
? | |
1.4.9.2 | n-butylamine + H2O + 2 blue protein | - |
Pseudomonas putida | butanal + NH3 + 2 blue protein | - |
? | |
1.4.9.2 | n-butylamine + H2O + 2 blue protein | - |
Pseudomonas putida IFO 15366 | butanal + NH3 + 2 blue protein | - |
? | |
1.4.9.2 | propylamine + H2O + 2 blue protein | the azurin-like blue protein is reduced specifically during AMDH reaction. The amine oxidation system can be reconstituted using AMDH, blue protein, and the cytoplasmic membranes of the organism | Pseudomonas putida | propanal + NH3 + 2 blue protein | - |
? | |
1.4.9.2 | propylamine + H2O + 2 blue protein | the azurin-like blue protein is reduced specifically during AMDH reaction. The amine oxidation system can be reconstituted using AMDH, blue protein, and the cytoplasmic membranes of the organism | Pseudomonas putida IFO 15366 | propanal + NH3 + 2 blue protein | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.4.9.2 | trimer | 1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE | Pseudomonas putida |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.9.2 | AMDH | - |
Pseudomonas putida |
1.4.9.2 | quinohemoprotein amine dehydrogenase | - |
Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.9.2 | heme c | two mol of heme per mole of AMDH, 60 kDa subunit carries heme c. Typical absorption stectrum shows maxima at 554, 522, 420, and 320 nm in the reduced state and one peak at 410 nm, a shoulder at 350 nm, and a braod hill at 530 nm in the oxidized form | Pseudomonas putida |