BRENDA - Reference to 1.4.9.2; Id = 714515

-

Pseudomonas putida

2,4-Dinitrophenylhydrazine

-

Pseudomonas putida

4-nitrophenylhydrazine

-

Pseudomonas putida

hydroxylamine

-

Pseudomonas putida

Semicarbazide

-

Pseudomonas putida

20000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

40000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

60000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

120000

-

gel filtration and sedimentation equilibrium analysis

Pseudomonas putida

P0A182

catalytic subunit

-

Pseudomonas putida IFO 15366

P0A182

catalytic subunit

-

13

-

25°C, pH 8.0

Pseudomonas putida

n-amylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida

? + NH3 + 2 blue protein

-

?

n-amylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida IFO 15366

? + NH3 + 2 blue protein

-

?

n-butylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida

butanal + NH3 + 2 blue protein

-

?

n-butylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida IFO 15366

butanal + NH3 + 2 blue protein

-

?

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

714515

Pseudomonas putida

propanal + NH3 + 2 blue protein

-

?

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

714515

Pseudomonas putida IFO 15366

propanal + NH3 + 2 blue protein

-

?

trimer

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

AMDH

-

Pseudomonas putida

quinohemoprotein amine dehydrogenase

-

Pseudomonas putida

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

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

-

Pseudomonas putida

2,4-Dinitrophenylhydrazine

-

Pseudomonas putida

4-nitrophenylhydrazine

-

Pseudomonas putida

hydroxylamine

-

Pseudomonas putida

Semicarbazide

-

Pseudomonas putida

20000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

40000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

60000

-

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

120000

-

gel filtration and sedimentation equilibrium analysis

Pseudomonas putida

13

-

25°C, pH 8.0

Pseudomonas putida

n-amylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida

? + NH3 + 2 blue protein

-

?

n-amylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida IFO 15366

? + NH3 + 2 blue protein

-

?

n-butylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida

butanal + NH3 + 2 blue protein

-

?

n-butylamine + H2O + 2 blue protein

-

714515

Pseudomonas putida IFO 15366

butanal + NH3 + 2 blue protein

-

?

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

714515

Pseudomonas putida

propanal + NH3 + 2 blue protein

-

?

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

714515

Pseudomonas putida IFO 15366

propanal + NH3 + 2 blue protein

-

?

trimer

1 * 60000, 1 * 40000, 1 * 20000, SDS-PAGE

Pseudomonas putida

685206

Hothi

Catalysis by the isolated tryp ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

Biochemistry

47

183-194

2008

-

1

-

10

-

1

-

1

-

8

-

2

-

1

-

1

-

1

-

1

-

1

-

8

-

685188

Hothi

Isotope effects reveal that pa ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

Biochemistry

46

9250-9259

2007

-

1

-

9

-

1

-

1

-

4

1

2

-

1

-

1

-

1

-

1

-

4

1

-

687589

Roujeinikova

New insights into the reductiv ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

J. Biol. Chem.

282

23766-23777

2007

-

2

-

9

-

1

-

8

1

2

-

1

-

1

-

2

-

1

-

8

1

-

672092

Sukumar

Crystal structure of an electr ...

Alcaligenes faecalis

Biochemistry

45

13500-13510

2006

-

1

-

3

-

1

-

673559

Hothi

Tryptophan tryptophylquinone c ...

Alcaligenes faecalis

FEBS J.

273

430

2006

-

3

-

1

-

1

-

1

-

2

-

2

-

3

-

1

-

1

-

2

-

2

-

674733

Roujeinikova

Atomic level insight into the ...

Alcaligenes faecalis

J. Biol. Chem.

281

40264-40272

2006

-

1

-

2

-

1

-

1

-

677123

Massgrau

Atomic description of an enzym ...

Alcaligenes faecalis

Science

312

237-241

2006

-

1

-

1

-

655062

Kondo

Purification and characterizat ...

Achromobacter xylosoxidans, Achromobacter xylosoxidans IFO13495

Biosci. Biotechnol. Biochem.

68

1921-1928

2004

-

15

4

-

3

2

-

3

-

1

-

1

23

1

2

1

3

-

1

-

1

-

1

-

15

-

4

-

3

2

-

1

-

1

23

1

3

-

1

-

1

-

396596

Chistoserdov

Cloning, sequencing and mutage ...

Achromobacter xylosoxidans, Alcaligenes faecalis

Microbiology

147

2195-2202

2001

-

1

-

2

-

5

-

2

-

1

2

-

1

-

2

-

2

-

1

-

396595

Hyun

Gated and ungated electron tra ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

J. Biol. Chem.

274

29081-29086

1999

-

2

-

10

-

4

-

1

-

1

-

2

-

4

-

715340

Zhu

Localization of periplasmic re ...

Alcaligenes faecalis

J. Bacteriol.

181

6540-6542

1999

-

1

-

1

-

3

-

1

-

1

-

714515

Adachi

-

Characterization of quinohemop ...

Pseudomonas putida, Pseudomonas putida IFO 15366

Biosci. Biotechnol. Biochem.

62

469-478

1998

-

1

-

4

-

4

-

2

-

1

-

6

1

2

-

1

-

1

-

4

-

4

-

1

-

6

1

-

396593

Hyun

Electron transfer reactions be ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

Biochemistry

34

12249-12254

1995

-

2

-

2

-

10

-

6

-

2

-

1

-

1

-

2

-

2

-

6

-

2

-

396594

Hyun

Unusually large isotope effect ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

Biochim. Biophys. Acta

1251

198-200

1995

-

2

-

9

-

2

-

2

-

2

-

2

-

2

-

715426

Edwards

Spectroscopic evidence for a c ...

Alcaligenes faecalis

J. Biol. Chem.

270

4293-4298

1995

-

1

-

4

-

1

-

1

-

1

-

1

-

1

-

396592

Govindaraj

Aromatic amine dehydrogenase, ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

J. Bacteriol.

176

2922-2929

1994

-

1

8

3

-

4

-

9

-

1

-

2

-

6

1

-

1

-

1

3

-

1

-

1

-

8

3

-

4

-

1

-

2

-

6

1

-

1

-

288289

Cuskey

Initial catabolism of aromatic ...

Pseudomonas aeruginosa

J. Bacteriol.

169

2398-2404

1987

-

1

-

1

-

1

-

3

-

3

-

1

-

1

-

1

-

3

-

396589

Nozaki

Aromatic amine dehydrogenase f ...

Alcaligenes faecalis, Alcaligenes faecalis IFO 14479

Methods Enzymol.

142

650-655

1987

-

1

-

3

-

3

-

10

-

1

-

1

-

10

1

-

1

-

1

-

1

-

3

-

3

-

1

-

1

-

10

1

-

396591

Iwaki

Crystallization and properties ...

Pseudomonas sp.

Arch. Biochem. Biophys.

220

253-262

1983

-

1

-

6

4

-

2

3

-

5

-

1

-

1

-

10

1

-

2

1

-

1

-

6

-

4

-

2

3

-

1

-

1

-

10

1

-

2

1

-

Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas putida

Data extracted from this reference: