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Literature summary extracted from

  • Adachi, O.; Kubota, T.; Hacisalihoglu, A.; Toyama, H.; Shinagawa, E.; Duine, J.; Matsushita, K.
    Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas putida (1998), Biosci. Biotechnol. Biochem., 62, 469-478.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.4.9.2
-
 Pseudomonas putida

Inhibitors

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

Molecular Weight [Da]

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

Organism

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
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.9.2 trimer 1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.4.9.2 AMDH
-
 Pseudomonas putida
1.4.9.2 quinohemoprotein amine dehydrogenase
-
 Pseudomonas putida

Cofactor

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