print visible entries

print all entries

Ligand 2-phenylethylamine

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (9 results)

top print hide

Show Natural Substrate (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.8

phenethylamine + NADPH + O2 = phenethylamine N-oxide + NADP+ + H2O

676315

-

1.4.3.21

2-phenylethylamine + H2O + O2 = beta-phenylethanal + NH3 + H2O2

703130

-

1.4.3.21

phenylethyl amine + H2O + O2 = phenylethanal + NH3 + H2O2

705496

-

1.4.3.4

2-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

711832, 725620

-

1.4.3.4

2-phenylethylamine + H2O + O2 = ?

711407, 711912

-

1.4.3.4

phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

705901, 706602

-

1.4.3.21

2 entries

1.4.3.4

3 entries

1.4.9.1

2-phenylethylamine + 2 H2O + 2 acceptor = 2-phenylacetic acid + NH3 + 2 reduced acceptor

686425

-

1.4.9.2

beta-phenylethylamine + H2O + 2,6-dichlorophenol indophenol = phenylacetaldehyde + NH3 + reduced 2,6-dichlorophenol indophenol

655062

-

2.3.1.87

acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine

720470, 720933

5gi6, 3D-view

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

top print hide

Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.1.28

L-phenylalanine = 2-phenylethylamine + CO2

0

-

4.1.1.28

L-phenylalanine = phenylethylamine + CO2

0

-

4.1.1.28

phenylalanine = phenylethylamine + CO2

0

-

4.1.1.28

3 entries

4.1.1.53

L-phenylalanine = phenylethylamine + CO2

0

-

Substrate in Enzyme-catalyzed Reactions (53 results)

top print hide

Show Substrate (53 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

phenylethylamine + ? = ?

286164

-

1.14.13.8

phenethylamine + NADPH + O2 = phenethylamine N-oxide + NADP+ + H2O

676315

-

1.14.17.1

2-phenylethylamine + ascorbate + O2 = ?

438610

-

1.14.17.1

phenylethylamine + ascorbate + O2 = ? + dehydroascorbate + H2O

659287

-

1.14.17.1

2 entries

1.4.1.28

phenethylamine + H2O + NAD+ = acetophenone + NH3 + NADH + H+

763366

-

1.4.3.21

2-phenylethanamine + H2O + O2 = ? + NH3 + H2O2

686264

-

1.4.3.21

2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + NH3 + H2O2

743457

-

1.4.3.21

2-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

654501, 724322, 655782, 671976, 672146, 687276, 724280

-

1.4.3.21

2-phenylethylamine + H2O + O2 = ?

726536

-

1.4.3.21

2-phenylethylamine + H2O + O2 = beta-phenylethanal + NH3 + H2O2

703130

-

1.4.3.21

2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2

742881, 726536, 725314, 742933

-

1.4.3.21

beta-phenylethylamine + H2O + O2 = beta-phenylethanal + NH3 + H2O2

675286

-

1.4.3.21

beta-phenylethylamine + O2 + H2O = beta-phenylethanal + NH3 + H2O2

672492

-

1.4.3.21

phenethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2

726290

-

1.4.3.21

phenylethyl amine + H2O + O2 = phenylethanal + NH3 + H2O2

705496

-

1.4.3.21

phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2

743594, 743371, 725733

-

1.4.3.22

2-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

391941, 672200, 391951

-

1.4.3.22

2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2

672200

-

1.4.3.22

beta-phenylethylamine + O2 + H2O = beta-phenylethanal + NH3 + H2O2

672492

-

1.4.3.22

phenylethylamine + H2O + O2 = ?

725736

-

1.4.3.22

phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2

672200, 723927

-

1.4.3.22

phenylethylamine + H2O + O2 = phenylethanal + NH3 + H2O2

688193

-

1.4.3.4

2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + NH3 + H2O2

723891

-

1.4.3.4

2-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

655187, 394553, 394555, 394572, 394556, 394562, 394567, 394569, 656607, 656683, 706602, 394559, 394570, 394577, 394576, 391951, 711832, 742990, 742989, 713457, 742988, 394552, 672153, 720626, 725621, 725622, 725620, 394566, 394579, 394574, 394580, 672492, 720287, 724603

-

1.4.3.4

2-phenylethylamine + H2O + O2 = ?

711407, 711912

-

1.4.3.4

beta-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

706934

-

1.4.3.4

beta-phenylethylamine + H2O + O2 = beta-phenylethanal + NH3 + H2O2

675286

-

1.4.3.4

beta-phenylethylamine + O2 + H2O = beta-phenylethanal + NH3 + H2O2

672492

-

1.4.3.4

phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

656047, 705901, 672525, 688478, 688481, 688492, 675073, 703627, 703657, 706602

-

1.4.3.4

phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2 + NH3 + H2O2

724966

-

1.4.3.4

phenylethylamine + H2O + O2 = phenylethanal + NH3 + H2O2

689175

-

1.4.9.1

2-phenylethylamine + 2 H2O + 2 acceptor = 2-phenylacetic acid + NH3 + 2 reduced acceptor

686425

-

1.4.9.1

2-phenylethylamine + acceptor + H2O = 2-phenylacetaldehyde + NH3 + reduced acceptor

654676

-

1.4.9.1

phenylethylamine + acceptor + H2O = phenylacetaldehyde + NH3 + reduced acceptor

396585, 396571, 685296

-

1.4.9.2

2-phenylethylamine + H2O + 2,6-dichlorophenolindophenol = phenylacetaldehyde + NH3 + reduced 2,6-dichlorophenolindophenol

396591

-

1.4.9.2

beta-phenylethylamine + acceptor + H2O = ? + NH3 + reduced acceptor

396596

-

1.4.9.2

beta-phenylethylamine + H2O + 2,6-dichlorophenol indophenol = phenylacetaldehyde + NH3 + reduced 2,6-dichlorophenol indophenol

655062

-

1.4.9.2

beta-phenylethylamine + H2O + 2,6-dichlorophenolindophenol = phenylacetaldehyde + NH3 + reduced 2,6-dichlorophenolindophenol

687589

-

1.4.9.2

phenylethylamine + acceptor + H2O = phenylacetaldehyde + NH3 + reduced acceptor

685188, 685206

-

1.4.3.21

11 entries

1.4.3.22

6 entries

1.4.3.4

9 entries

1.4.9.1

3 entries

1.4.9.2

5 entries

1.5.3.5

2-phenylethylamine + H2O + O2 = 2-phenylethanal + NH3 + H2O2

726378

-

2.1.1.49

S-adenosyl-L-methionine + beta-phenylethylamine = ?

441353

-

2.3.1.110

feruloyl-CoA + beta-phenylethylamine = CoA + feruloyl-beta-phenylethylamine

486132

-

2.3.1.110

4-coumaroyl-CoA + phenethylamine = CoA + N-(4-coumaroyl)phenethylamine

720789

-

2.3.1.110

feruloyl-CoA + phenethylamine = CoA + feruloylphenethylamine

486130, 660244

-

2.3.1.110

3 entries

2.3.1.5

acetyl-CoA + beta-phenylethylamine = CoA + N-(2-phenylethyl)-acetaminde

487129, 487120, 487628, 487107, 487126

-

2.3.1.57

acetyl-CoA + beta-phenylethylamine = CoA + N-acetylphenylethylamine

487256

-

2.3.1.87

acetyl-CoA + 2-phenylethylamine = CoA + N-acetyl-2-phenylethylamine

660441

5gi6, 3D-view

2.3.1.87

acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine

720470, 720933

5gi6, 3D-view

2.3.1.87

acetyl-CoA + beta-phenylethylamine = CoA + N-(2-phenylethyl)-acetaminde

487126, 487644, 487621, 487622, 487634, 487629

5gi6, 3D-view

2.3.1.87

acetyl-CoA + phenethylamine = CoA + N-acetyl-phenethylamine

735681

5gi6, 3D-view

2.3.1.87

acetyl-CoA + phenylethylamine = CoA + N-acetyl-phenylethylamine

658645, 658812

5gi6, 3D-view

2.3.1.87

acetyl-CoA + phenylethylamine = CoA + N-acetylphenylethylamine

735933, 758432, 720470, 736685

5gi6, 3D-view

2.3.1.87

6 entries

2.6.1.116

2-phenylethylamine + pyruvate = 2-phenylethanal + L-alanine

753557

-

Product in Enzyme-catalyzed Reactions (13 results)

top print hide

Show Product (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.76

N-Acetyl-2-phenylethylamine + H2O = 2-Phenylethylamine + acetate

31889

-

4.1.1.14

L-Phe = 2-phenylethylamine + CO2

0, 3968

-

4.1.1.19

L-Phe = phenylethylamine + CO2

0

-

4.1.1.25

L-phenylalanine = beta-phenylethylamine + CO2

0

-

4.1.1.25

L-phenylalanine + H2O = phenylethylamine + H2O2

0

-

4.1.1.28

L-phenylalanine = 2-phenylethylamine + CO2

0

-

4.1.1.28

L-phenylalanine = L-phenethylamine + CO2

0

-

4.1.1.28

L-Phe = phenylethylamine + CO2

0

-

4.1.1.28

L-phenylalanine = phenylethylamine + CO2

650450, 653288, 0

-

4.1.1.28

phenylalanine = phenylethylamine + CO2

0

-

4.1.1.25

2 entries

4.1.1.28

5 entries

4.1.1.53

L-phenylalanine = phenylethylamine + CO2

0

-

4.1.1.B12

L-phenylalanine = phenylethylamine + CO2

0

-

4.3.2.9

5-L-glutamyl-beta-phenethylamine = 5-oxoproline + beta-phenethylamine

0

-

Inhibitor in Enzyme-catalyzed Reactions (26 results)

top print hide

Show Inhibitors (26 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.3

competitive inhibition

439347

-

1.14.18.1

-

696563

-

1.4.1.20

-

349651

-

1.4.1.20

competitive with L-Phe

349636

-

1.4.1.20

2 entries

1.4.3.10

-

395447

-

1.4.3.13

-

741494

-

1.4.3.21

substrate inhibition

703130, 726536

-

1.4.3.21

-

725733

-

1.4.3.21

2 entries

1.4.3.4

time-dependent, slowly reversible suicide inhibition. Addition of 2-phenylethylamine (10mM) to the enzyme results in immediate bleaching of the absorbance peak at 460 nm, a consequence of rapid reduction of the flavin cofactor by 2-phenylethylamine at steady state

720626

-

1.4.9.2

substrate inhibition

396591

-

1.4.9.2

substrate inhibition at higher concentrations

655062

-

2.1.1.28

-

696719

-

2.1.1.28

-

696719

-

2.1.1.28

competitive inhibition with respect to phenylethanolamine

639447

-

1.4.9.2

2 entries

2.1.1.28

3 entries

2.6.1.5

80% inhibition with tyrosine at 3 mM and phenylethylamine at 12 mM

640109

-

3.4.19.6

-

667505

-

3.4.21.4

-

653809

1tnj, 3D-view

3.4.21.4

-

653809

1utm, 3D-view

3.4.21.4

-

653809

1uto, 3D-view

3.4.21.4

3 entries

3.4.23.15

-

95789

-

3.5.1.88

-

719067

-

3.5.1.91

inhibits the reverse enzyme reaction

733172

-

4.1.1.28

competitive inhibition, 80% inhibition at 0.5 mM

743978

-

4.1.1.28

-

4208

-

4.1.1.28

2 entries

4.3.1.24

-

34364

-

6.3.1.6

-

958

-

3D Structure of Enzyme-Ligand-Complex (PDB) (77 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (77 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.11.1.7

4oek, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

1d6u, 3D-view

1.4.3.6

1d6y, 3D-view

1.4.3.6

1d6z, 3D-view

1.4.3.6

36 entries

1.4.99.4

2hkm, 3D-view

2.3.1.87

5gi6, 3D-view

3.4.21.36

4est, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

1tnj, 3D-view

3.4.21.4

1utm, 3D-view

3.4.21.4

1uto, 3D-view

3.4.21.4

36 entries

3.4.22.15

1mhw, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (64 results)

top print hide

Show Turnover Number (64 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.21

0.00021

-

pH 6.8, 30°C, mutant enzyme D298A

672146

1.4.3.21

0.00612

-

pH 8.0, mutant enzyme D383E

654501

1.4.3.21

0.00937

-

pH 7.0, mutant enzyme D383E

654501

1.4.3.21

0.01163

-

pH 5.5, mutant enzyme D383E

654501

1.4.3.21

0.012

-

pH 6.0, mutant enzyme D383E

654501

1.4.3.21

0.63

-

pH 6.8, 30°C, Ni-activated enzyme

671976

1.4.3.21

0.92

-

pH 6.8, 30°C, Co-activated enzyme

671976

1.4.3.21

1.12

-

at pH 7.4, 37°C

726290

1.4.3.21

1.3

-

pH 6.8, 30°C, Ni2+-substituted enzyme

655782

1.4.3.21

1.51

-

pH 6.8, 30°C, Co2+-substituted enzyme

655782

1.4.3.21

1.72

-

isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

1.4.3.21

5.12

-

isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

1.4.3.21

9.6

-

pH 5.5, wild-type enzyme

654501

1.4.3.21

11.45

-

pH 5.75, wild-type enzyme

654501

1.4.3.21

12.4

-

wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C

724280

1.4.3.21

13.32

-

pH 7.5, wild-type enzyme

654501

1.4.3.21

13.68

-

pH 8.0, wild-type enzyme

654501

1.4.3.21

14.98

-

pH 7.0, wild-type enzyme

654501

1.4.3.21

20.7

-

pH 6.0, wild-type enzyme

654501

1.4.3.21

20.77

-

pH 6.5, wild-type enzyme

654501

1.4.3.21

20.9

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

44

-

in 50mM HEPES buffer, pH 6.8, at 15°C

725314

1.4.3.21

75.7

-

pH 6.8, 30°C, Cu-activated enzyme

671976

1.4.3.21

75.7

-

pH 6.8, 30°C, native copper protein

655782

1.4.3.21

76

-

pH 6.8, 30°C, wild-type enzyme

672146

1.4.3.22

10.6

-

pH 7.2, 25°C

688193

1.4.3.22

11.2

-

30°C, pH 7.0, per dimer

672200

1.4.3.22

15.8

-

pH 7.2, 25°C

688193

1.4.3.22

30.9

-

pH 8.5, 25°C

688193

1.4.3.22

39.8

-

pH 8.5, 25°C

688193

1.4.3.22

44

-

30°C, pH 7.2, per dimer

672200

1.4.3.22

137

-

-

391951

1.4.3.4

0.012

-

pH 7.5, 25°C, mutant enzyme Y435W

672153

1.4.3.4

0.033

-

30°C, mutant enzyme Y402A

394556

1.4.3.4

0.066

-

pH 7.5, 25°C, mutant enzyme Y435H

672153

1.4.3.4

0.67

-

30°C, mutant enzyme Y410A

394556

1.4.3.4

0.79

-

pH 7.5, 25°C, mutant enzyme Y435L

672153

1.4.3.4

0.833

-

30°C, mutant enzyme Y402F

394556

1.4.3.4

0.87

-

pH 7.5, 25°C, mutant enzyme Y435F

672153

1.4.3.4

0.897

-

-

688481

1.4.3.4

0.897

-

pH 7.5, detergent solubilized MAO-A

688478

1.4.3.4

0.998

-

pH 7.5, MAO-A incorporated into phospholipid nanodisks

688478

1.4.3.4

1.17

-

30°C, mutant enzyme Y407F

394556

1.4.3.4

1.4

-

-

688481

1.4.3.4

1.42

-

isoform MAO A, in 50 mM potassium phosphate assay buffer (pH 7.5), at 25°C

706602

1.4.3.4

1.42

-

pH 7.5, 25°C, MAO-A

706602

1.4.3.4

1.481

-

11°C

394552

1.4.3.4

1.83

-

mutant enzyme I199A/Y326A, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

2

-

30°C, wild-type enzyme

394556

1.4.3.4

2.05

-

mutant enzyme I199A, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

2.5

-

pH 7.2, 30°C, mutant enzyme C374A

672525

1.4.3.4

2.87

-

wild type isoform MAO B, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

3.1

-

pH 7.2, 30°C, wild-type enzyme

672525

1.4.3.4

3.4

-

pH 7.4, 25°C

713457

1.4.3.4

3.82

-

pH 7.5, 25°C, wild-type enzyme

672153

1.4.3.4

18.2

20.8

MAO-B

394555

1.4.3.4

20.8

-

-

394576

1.4.9.1

3.1

-

pH 7.5, 30°C

654676

1.4.9.1

26

-

-

396585

2.3.1.87

7.2

-

cosubstrate acetyl-CoA, pH 7.0, 25°C

758432

2.3.1.87

42

-

wild-type, pH 8.0, 22°C

735681

2.6.1.116

0.3

-

pH 8.0, 30°C

753557

2.6.1.116

0.72

-

pH 8.0, 30°C

753557

2.6.1.116

0.75

-

pH 8.0, 30°C

753557

1.4.3.21

25 entries

1.4.3.22

7 entries

1.4.3.4

25 entries

1.4.9.1

2 entries

2.3.1.87

2 entries

2.6.1.116

3 entries

K_M Value (103 results)

top print hide

Show KM Value (103 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.17.1

7

-

-

438610

1.4.3.21

0.00088

-

pH 8.0, mutant enzyme D383E

654501

1.4.3.21

0.0012

-

wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C

724280

1.4.3.21

0.0012

-

pH 7.0, wild-type enzyme

654501

1.4.3.21

0.0017

-

pH 6.5, wild-type enzyme

654501

1.4.3.21

0.0017

-

pH 7.5, wild-type enzyme

654501

1.4.3.21

0.0018

-

pH 6.0, wild-type enzyme

654501

1.4.3.21

0.0019

-

pH 6.8, 30°C, Co2+-substituted enzyme

655782

1.4.3.21

0.0021

-

pH 6.8, 30°C, mutant enzyme D298A

672146

1.4.3.21

0.0023

-

pH 5.75, wild-type enzyme

654501

1.4.3.21

0.0023

-

pH 8.0, wild-type enzyme

654501

1.4.3.21

0.00247

-

pH 7.0, mutant enzyme D383E

654501

1.4.3.21

0.0025

-

in 50mM HEPES buffer, pH 6.8, at 15°C

725314

1.4.3.21

0.0025

-

pH 6.8, 30°C, Co-activated enzyme

671976

1.4.3.21

0.0025

-

pH 6.8, 30°C, Cu-activated enzyme

671976

1.4.3.21

0.0025

-

pH 6.8, 30°C, native copper protein

655782

1.4.3.21

0.0025

-

pH 6.8, 30°C, wild-type enzyme

672146

1.4.3.21

0.0034

-

pH 6.8, 30°C, Ni-activated enzyme

671976

1.4.3.21

0.0038

-

pH 6.8, 30°C, Ni2+-substituted enzyme

655782

1.4.3.21

0.0055

-

isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

1.4.3.21

0.0078

-

pH 5.5, wild-type enzyme

654501

1.4.3.21

0.00962

-

pH 6.0, mutant enzyme D383E

654501

1.4.3.21

0.012

-

isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

1.4.3.21

0.02

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

0.028

-

pH 5.5, mutant enzyme D383E

654501

1.4.3.21

0.077

-

recombinant enzyme expressed in CHO cells

703130

1.4.3.21

1.94

-

recombinant enzyme expressed in CHO cells

703130

1.4.3.21

2.05

-

at pH 7.4, 37°C

726290

1.4.3.21

3.7

5

at pH 7.0 and 37°C

743371

1.4.3.22

0.0015

-

30°C, pH 7.2

672200

1.4.3.22

0.039

-

30°C, pH 7.0

672200

1.4.3.22

0.12

-

-

391951

1.4.3.22

0.13

-

pH 7.2, 25°C

688193

1.4.3.22

0.84

-

immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C

723927

1.4.3.22

1.2

-

pH 7.2, 25°C

688193

1.4.3.22

1.3

-

pH 8.5, 25°C

688193

1.4.3.22

1.4

-

pH 8.5, 25°C

688193

1.4.3.4

0.0004

-

pH 7.4, 37°C, cerebral MAO-B

705901

1.4.3.4

0.0022

-

monoamine oxidase B wild-type enzyme

656047

1.4.3.4

0.0052

-

monoamine oxidase B mutant D123A

656047

1.4.3.4

0.0078

-

monoamine oxidase B mutant Y398F

656047

1.4.3.4

0.0094

-

wild type isoform MAO B, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

0.016

-

pH 7.5, 25°C, wild-type enzyme

672153

1.4.3.4

0.0208

-

-

394562

1.4.3.4

0.0211

-

monoamine oxidase B mutant Y435F

656047

1.4.3.4

0.022

-

-

394559

1.4.3.4

0.04

-

mutant enzyme I199A, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

0.0449

-

pH 7.4, 30°C, oxidative half-reaction

720626

1.4.3.4

0.048

-

-

394559

1.4.3.4

0.05

-

pH 7.5, 25°C, mutant enzyme Y435L

672153

1.4.3.4

0.13

-

pH 7.5, 25°C, mutant enzyme Y435F

672153

1.4.3.4

0.19

-

-

394576

1.4.3.4

0.19

0.25

MAO-B

394555

1.4.3.4

0.24

-

at pH 7.4 and 25°C

742988

1.4.3.4

0.29

-

at pH 7.4 and 25°C

742988

1.4.3.4

0.29

-

pH 7.5, 25°C, mutant enzyme Y435H

672153

1.4.3.4

0.35

-

isoform MAO A, in 50 mM potassium phosphate assay buffer (pH 7.5), at 25°C

706602

1.4.3.4

0.35

-

-

688481

1.4.3.4

0.35

-

pH 7.5, 25°C, MAO-A

706602

1.4.3.4

0.423

-

pH 7.4, 30°C, reductive half-reaction

720626

1.4.3.4

0.44

-

pH 7.2, 30°C, mutant enzyme C374A

672525

1.4.3.4

0.49

-

pH 7.2, 30°C, wild-type enzyme

672525

1.4.3.4

0.49

-

pH 7.5, MAO-A incorporated into phospholipid nanodisks

688478

1.4.3.4

0.57

-

30°C, wild-type enzyme

394556

1.4.3.4

0.68

-

pH 7.5, 25°C, mutant enzyme Y435W

672153

1.4.3.4

0.7

-

at pH 7.4 and 25°C

742988

1.4.3.4

0.703

-

mutant enzyme I199A/Y326A, at 25°C in 50 mM phosphate buffer (pH 7.5)

724966

1.4.3.4

0.71

-

at pH 7.0 and 37°C

723891

1.4.3.4

0.78

-

30°C, mutant enzyme Y402F

394556

1.4.3.4

0.89

-

11°C

394552

1.4.3.4

1.13

-

30°C, mutant enzyme Y410A

394556

1.4.3.4

1.2

-

at pH 7.4 and 25°C

742988

1.4.3.4

1.4

-

at pH 7.0 and 37°C

724603

1.4.3.4

1.42

-

30°C, mutant enzyme Y407F

394556

1.4.3.4

1.48

-

-

688481

1.4.3.4

1.48

-

pH 7.5, detergent solubilized MAO-A

688478

1.4.3.4

1.98

-

30°C, mutant enzyme Y402A

394556

1.4.3.4

3.6

-

-

394577

1.4.3.4

4.3

-

in 0.01 M phosphate buffer, pH 7.4, at 23°C

725620

1.4.3.4

6.3

-

at pH 7.4 and 25°C

742990

1.4.3.4

6.34

-

pH not specified in the publication, temperature not specified in the publication

711832

1.4.3.4

8.13

-

at pH 7.4 and 25°C

742989

1.4.3.4

86

-

pH 7.4, 25°C

713457

1.4.9.2

0.0018

-

pH 7.5, 30°C

655062

1.4.9.2

0.0045

-

-

396591

1.4.3.21

28 entries

1.4.3.22

8 entries

1.4.3.4

46 entries

1.4.9.2

2 entries

2.1.1.49

6.25

-

5-methyltetrahydrofolate as methyl donor

441353

2.3.1.110

0.112

-

with 4-coumaroyl-CoA, pH 7.5, 30°C, recombinant AAT1

720789

2.3.1.110

0.57

-

with feruloyl-CoA as acceptor

486130

2.3.1.110

1.389

-

pH 8.5, 30°C

660244

2.3.1.110

4.276

-

-

486132

2.3.1.5

0.18

-

-

487120

2.3.1.5

0.3

-

-

487120

2.3.1.87

0.009

-

-

487634

2.3.1.87

0.17

-

pH 6.8, 37°C

660441

2.3.1.87

0.173

-

-

487644

2.3.1.87

0.32

-

wild-type, pH 8.0, 22°C

735681

2.3.1.87

0.34

-

-

658812

2.3.1.87

1.8

-

pH 6.8, 37°C

660441

2.3.1.87

9.5

-

pH 6.8, 37°C

660441

2.3.1.87

11

-

cosubstrate acetyl-CoA, pH 7.0, 25°C

758432

2.6.1.116

3.6

-

pH 8.0, 30°C

753557

2.6.1.116

5

-

pH 8.0, 30°C

753557

2.6.1.116

81

-

pH 8.0, 30°C

753557

2.3.1.110

4 entries

2.3.1.5

2 entries

2.3.1.87

8 entries

2.6.1.116

3 entries

K_i Value (9 results)

top print hide

Show KI Value (9 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.1.20

1.52

-

-

349636

1.4.3.10

0.087

-

-

395447

1.4.3.21

0.08

-

recombinant enzyme expressed in CHO cells

703130

1.4.3.21

0.6

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

0.84

-

isoform AMAO2, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

1.4.3.21

1.41

-

isoform AMAO3, in 100 mM potassium phosphate buffer (pH 7.0), at 37°C

726536

2.1.1.28

0.22

-

pH 8.0, 37°C

696719

2.1.1.28

3.6

-

competitive with phenylethanolamine

639447

1.4.3.21

4 entries

2.1.1.28

2 entries

3.4.19.6

0.00398

-

-

667505

IC₅₀ Value (5 results)

top print hide

Show IC50 Value (5 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.4.3.13

0.0601

-

LOXL2 protein, at pH 8.0 and 37°C

741494

3.5.1.88

0.00000012

-

in 50 mM potassium phosphate (pH 7.6), at 25°C

719067

3.5.1.88

0.00000086

-

in 50 mM potassium phosphate (pH 7.6), at 25°C

719067

3.5.1.88

0.0000036

-

in 50 mM potassium phosphate (pH 7.6), at 25°C

719067

3.5.1.88

3 entries

3.5.1.91

27.8

-

pH 7.0, 25°C

733172

References & Links

Literature References (139)

top print hide

Show Reference (139 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

958

-

Some properties of the theanine synthesizing enzyme in tea seedlings

1965

Sasaoka, K.; Kito, M.; Onishi, Y.

Agric. Biol. Chem.

29

984-988

3968

-

Leucin-carboxylase aus marinen Rhodophyceae: Vorkommen, Verbreitung und einige Eigenschaften

1972

Hartmann, T.

Phytochemistry

11

1327-1336

4208

-

Inhibition of aromatic L-amino acid decarboxylase from Micrococcus percitreus by substrate analogs

1987

Nakazawa, H.; Kumagai, H.; Yamada, H.

Agric. Biol. Chem.

51

2531-2537

31889

1396711

Purification and characterization of a novel enzyme, arylalkyl acylamidase, from Pseudomonas putida Sc2

1992

Shimizu, S.; Ogawa, J.; Chung, M.C.M.; Yamada, H.

Eur. J. Biochem.

209

375-382

34364

8043606

Phenylalanine ammonia-lyase from cotton (Gossypium hirsutum) hypocotyls: properties of the enzyme induced by a Verticillium dahliae phytotoxin

1994

Dubery, I.A.; Smit, F.

Biochim. Biophys. Acta

1207

24-30

95789

678526

Interaction of kidney renin with aryl-, isoalkyl-, and N-alkyl-substituted sepharose derivatives: Multiplicity of interaction sites

1978

Dworschack, R.T.; Printz, M.P.

Biochemistry

17

2484-2489

286164

4393513

Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain

1970

Tabakoff, B.; Erwin, G.

J. Biol. Chem.

245

3263-3268

349636

2536657

Purification and characterization of a dimeric phenylalanine dehydrogenase from Rhodococcus maris K-18

1989

Misono, H.; Yonezawa, J.; Nagata, S.; Nagasaki, S.

J. Bacteriol.

171

30-36

349651

10924111

Rhodococcus L-Phenylalanine Dehydrogenase: Kinetics, Mechanism, and Structural Basis for Catalytic Specificity

2000

Brunhuber, N.M.W.; Thoden, J.B.; Blanchard, J.S.; Vanhooke, J.L.

Biochemistry

39

9174-9187

391941

-

Purification and properties of the diamine oxidase from Vicia faba leaves

1981

Matsuda, H.; Suzuki, Y.

Plant Cell Physiol.

22

737-746

391951

7727530

Amine oxidases from Aspergillus niger: identification of a novel flavin-dependent enzyme

1995

Schilling, B.; Lerch, K.

Biochim. Biophys. Acta

1243

529-537

394552

11812236

High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae

2002

Li, M.; Hubalek, F.; Newton-Vinson, P.; Edmondson, D.E.

Protein Expr. Purif.

24

152-162

394553

11732903

Loss of serotonin oxidation as a component of the altered substrate specificity in the Y444F mutant of recombinant human liver MAO A

2001

Nandigama, R.K.; Miller, J.R.; Edmondson, D.E.

Biochemistry

40

14839-14846

394555

2037155

The kinetic mechanisms of monoamine oxidases A and B

1991

Ramsay, R.R.; Singer, T.P.

Biochem. Soc. Trans.

19

219-223

394556

11754741

Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A

2002

Ma, J.; Ito, A.

J. Biochem.

131

107-111

394559

5169190

The kinetics of phenethylhydrazine oxidation by monoamine oxidase

1971

Tipton, K.F.; Spires, I.P.C.

Biochem. J.

125

521-524

394562

4850215

A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes

1974

Houslay, M.D.; Tipton, K.F.

Biochem. J.

139

645-652

394566

6870271

Human brain monoamine oxidase: solubilization and kinetics of inhibition by octylglucoside

1983

Pearce, L.B.; Roth, J.A.

Arch. Biochem. Biophys.

224

464-472

394567

7081997

Purification of rat liver monoamine oxidase by octyl glucoside extraction and reconstitution

1982

Stadt, M.A.; Banks, P.A.; Kobes, R.D.

Arch. Biochem. Biophys.

214

223-230

394569

708051

Properties of a monoamine oxidase from rat liver mitochondrial outer membranes

1978

McCauley, R.

Arch. Biochem. Biophys.

189

8-13

394570

3096981

Modulation by phospholipids of the activity of monoamine oxidase purified from pig liver

1986

Inagaki, T.; Rao, N.A.; Yagi, K.

J. Biochem.

100

597-603

394572

2503040

Characterization of monoamine oxidase activity present in human granulocytes and lymphocytes

1989

Balsa, M.D.; Gomez, N.; Unzeta, M.

Biochim. Biophys. Acta

992

140-144

394574

3037268

Assay and purification of liver monoamine oxidase

1987

Youdim, M.B.H.; Tenne, M.

Methods Enzymol.

142

617-627

394576

7066309

Kinetic studies on the catalytic mechanism of liver monoamine oxidase

1982

Husain, M.; Edmondson, D.E.; Singer, T.P.

Biochemistry

21

595-600

394577

4434991

Kinetics of the interaction between pig-plasma benzylamine oxidase and various monoamines

1974

Lindström, A.; Olsson, B.; Petterson, G.; Szymanska, J.

Eur. J. Biochem.

47

99-105

394579

7447482

Kinetic properties of membrane-bound and Triton X-100-solubilized human brain monoamine oxidase

1980

Roth, J.A.; Eddy, B.J.

Arch. Biochem. Biophys.

205

260-266

394580

434814

Monoamine oxidase from beef liver mitochondria: simplified isolation procedure, properties, and determination of its cysteinyl flavin content

1979

Salach, J.I.

Arch. Biochem. Biophys.

192

128-137

395447

1260033

Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens

1976

Swain, W.F.; Desa, R.J.

Biochim. Biophys. Acta

429

331-341

396571

-

Crystallization and properties of amine dehydrogenase from Pseudomonas sp.

1988

Shinagawa, E.; Matsushita, K.; Nakashima, K.; Adachi, O.; Ameyama, M.

Agric. Biol. Chem.

52

2255-2263

396585

10346915

Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans

1999

Takagi, K.; Torimura, M.; Kawaguchi, K.; Kano, K.; Ikeda, T.

Biochemistry

38

6935-6942

396591

6830237

Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp

1983

Iwaki, M.; Yagi, T.; Horiike, K.; Saeki, Y.; Ushijima, T.; Nozaki, M.

Arch. Biochem. Biophys.

220

253-262

396596

11495996

Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases

2001

Chistoserdov, A.Y.

Microbiology

147

2195-2202

438610

6860408

Dopamine-beta-hydroxylase: suicide inhibition by the novel olefinic substrate, 1-phenyl-1-aminomethylethene

1983

May, S.W.; Mueller, P.W.; Padgette, S.R.; Herman, H.H.; Phillips, R.S.

Biochem. Biophys. Res. Commun.

110

161-168

439347

7840624

Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli

1995

Emanuele, J.J.; Heasley, C.J.; Fitzpatrick, P.F.

Arch. Biochem. Biophys.

316

241-248

441353

4766261

Multiple N-methyltransferases for aromatic alkylamines in brain

1973

Hsu, L.L.; Mandell, A.J.

Life Sci.

13

847-858

486130

10879473

Induction of N-hydroxycinnamoyltyramine synthesis and tyramine N-hydroxycinnamoyltransferase (THT) activity by wounding in maize leaves

2000

Ishihara, A.; Kawata, N.; Matsukawa, T.; Iwamura, H.

Biosci. Biotechnol. Biochem.

64

1025-1031

486132

9288939

Purification, characterization and partial amino acid sequencing of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase from tobacco cell-suspension cultures

1997

Negrel, J.; Javelle, F.

Eur. J. Biochem.

247

1127-1135

487107

-

Arylamine N-acetyltransferase from the chicken kidney: characterization of the enzyme and localization of the mRNA by in situ hybridization

1990

Ohtomi, M.; Tomoyuki, I.; Deguchi, T.

Biomed. Res.

11

263-267

487120

44212

N-Acylation of tyramines: purification and characterization of an arylamine N-acetyltransferase from rat brain and liver

1979

Yu, P.H.; Boulton, A.A.

Can. J. Biochem.

57

1204-1209

487126

2583181

Two arylamine N-acetyltransferases from chicken pineal gland as identified by cDNA cloning

1989

Ohtomi, M.; Sasaki, M.; Deguchi, T.

Eur. J. Biochem.

185

253-261

487129

2897359

Arylamine N-acetyltransferase from chicken liver. I. Monoclonal antibodies, immunoaffinity purification, and amino acid sequences

1988

Deguchi, T.; Sakamoto, Y.; Sasaki, Y.; Uyemura, K.

J. Biol. Chem.

263

7528-7533

487256

3987688

The occurrence, subcellular localization and partial purification of diamine acetyltransferase in the yeast Candida boidinii grown on spermidine or putrescine as sole nitrogen source

1985

Haywood, G.W.; Large, P.J.

Eur. J. Biochem.

148

277-283

487621

3298986

Arylalkylamine N-acetyltransferase from mammalian pineal gland

1987

Namboodiri, M.A.A.; Dubbels, R.; Klein, D.C.

Methods Enzymol.

142

583-590

487622

6469990

Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland

1984

Voisin, P.; Namboodiri, M.A.A.; Klein, D.C.

J. Biol. Chem.

259

10913-10918

487628

3625455

Multiple forms of arylalkylamine N-acetyltransferases in the rat pineal gland: purification of one molecular form

1987

Namboodiri, M.A.A.; Brownstein, M.J.; Weller, J.L.; Voisin, P.; Klein, D.C.

J. Pineal Res.

4

235-246

487629

167124

Characteristics of serotonin-acetyl coenzyme A N-acetyltransferase in pineal gland of rat

1975

Deguchi, T.

J. Neurochem.

24

1083-1085

487634

8740555

Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus

1996

Aisien, S.O.; Hellmund, C.; Walter, R.D.

Parasitol. Res.

82

369-371

487644

10722724

Substrate specificity and inhibition studies of human serotonin N-acetyltransferase

2000

Ferry, G.; Loynel, A.; Kucharczyk, N.; Bertin, S.; Rodriguez, M.; Delagrange, P.; Galizzi, J.P.; Jacoby, E.; Volland, J.P.; Lesieur, D.; Renard, P.; Canet, E.; Fauchere, J.L.; Boutin, J.A.

J. Biol. Chem.

275

8794-8805

639447

1167462

Substrate and inhibitor kinetics of bovine phenylethanolamine-N-methyltransferase

1975

Hoffman, A.R.; Ciaranello, R.D.; Axelrod, J.

Biochem. Pharmacol.

24

544-546

640109

14171223

Studies on the specificity of tyrosine-alpha-ketoglutarate transaminase

1964

Jacoby, G.A.; La Du, B.N.

J. Biol. Chem.

239

419-424

650450

11258661

Identification and characterization of an aromatic amino acid decarboxylase from the filarial nematode, Dirofilaria immitis

2001

Tang, L.; Frank, G.

Biol. Chem.

382

115-122

653288

100448768

First fungal aromatic L-amino acid decarboxylase from a paclitaxel-producing Penicillium raistrickii

1999

Niedens, B.R.; Parker, S.R.; Stierle, D.B.; Stierle, A.A.

Mycologia

91

619-626

653809

15044735

Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements

2004

Leiros, H.K.S.; Brandsdal, B.O.; Andersen, O.A.; Os, V.; Leiros, I.; Helland, R.; Otlewski, J.; Willassen, N.P.; Smalas, A.O.

Protein Sci.

13

1056-1070

654501

11985492

Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue

2002

Saysell, C.G.; Tambyrajah, W.S.; Murray, J.M.; Phillips, S.V.; McPherson, M.J.; Knowles, P.F.

Biochem. J.

365

809-816

654676

12974623

Chemical and kinetic reaction mechanisms of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans

2003

Sun, D.; Ono, K.; Okajima, T.; Tanizawa, K.; Uchida, M.; Yamamoto, Y.; Mathews, F.S.; Davidson, V.L.

Biochemistry

42

10896-10903

655062

15388968

Purification and characterization of aromatic amine dehydrogenase from Alcaligenes xylosoxidans

2004

Kondo, T.; Kondo, E.; Maki, H.; Yasumoto, K.; Takagi, K.; Kano, K.; Ikeda, T.

Biosci. Biotechnol. Biochem.

68

1921-1928

655187

11979502

Monoamine oxidase A and B activities in embryonic chick hepatocytes: differential regulation by retinoic acid

2002

Nicotra, A.; Falasca, L.; Senatori, O.; Devirgiliis, L.C.

Cell Biochem. Funct.

20

87-94

655782

12537504

Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes

2003

Kishishita, S.; Okajima, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Suzuki, S.; Kuroda, S.; Tanizawa, K.; Mure, M.

J. Am. Chem. Soc.

125

1041-1055

656047

11861643

Analysis of conserved active site residues in monoamine oxidase A and B and their three-dimensional molecular modeling

2002

Geha, R.M.; Chen, K.; Wouters, J.; Ooms, F.; Shih, J.C.

J. Biol. Chem.

277

17209-17216

656607

12686747

Inhibition by Zn2+ of A-form monoamine oxidase in monkey brain mitochondria

2003

Egashira, T.; Takayama, F.; Sakai, K.

J. Pharm. Sci.

91

239-245

656683

12818349

Differential substrate specificity of monoamine oxidase in the rat heart and renal cortex

2003

Guimaraes, J.T.; Vindis, C.; Soares-da-Silva, P.; Parini, A.

Life Sci.

73

955-967

658645

14717709

New substrate analogues of human serotonin N-acetyltransferase produce in situ specific and potent inhibitors

2004

Ferry, G.; Ubeaud, C.; Mozo, J.; Pean, C.; Hennig, P.; Rodriguez, M.; Scoul, C.; Bonnaud, A.; Nosjean, O.; Galizzi, J.P.; Delagrange, P.; Renard, P.; Volland, J.P.; Yous, S.; Lesieur, D.; Boutin, J.A.

Eur. J. Biochem.

271

418-428

658812

15302263

Duality of serotonin-N-acetyltransferase in the gilthead seabream (Sparus aurata): molecular cloning and characterization of recombinant enzymes

2004

Zilberman-Peled, B.; Benhar, I.; Coon, S.L.; Ron, B.; Gothilf, Y.

Gen. Comp. Endocrinol.

138

139-147

659287

12966104

Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase: Implications for the reactive oxygen species

2003

Evans, J.P.; Ahn, K.; Klinman, J.P.

J. Biol. Chem.

278

49691-49698

660244

15122017

Production of coumaroylserotonin and feruloylserotonin in transgenic rice expressing pepper hydroxycinnamoyl-coenzyme a:Serotonin N-(hydroxycinnamoyl)transferase

2004

Jang, S.M.; Ishihara, A.; Back, K.

Plant Physiol.

135

346-356

660441

15477086

Purification of the recombinant human serotonin N-acetyltransferase (EC 2.3.1.87): further characterization of and comparison with AANAT from other species

2004

Ferry, G.; Ubeaud, C.; Dauly, C.; Mozo, J.; Guillard, S.; Berger, S.; Jimenez, S.; Scoul, C.; Leclerc, G.; Yous, S.; Delagrange, P.; Boutin, J.A.

Protein Expr. Purif.

38

84-98

667505

15799721

Structure-activity studies with high-affinity inhibitors of pyroglutamyl-peptidase II

2005

Kelly, J.A.; Scalabrino, G.A.; Slator, G.R.; Cullen, A.A.; Gilmer, J.F.; Lloyd, D.G.; Bennett, G.W.; Bauer, K.; Tipton, K.F.; Williams, C.H.

Biochem. J.

389

569-576

671976

16142901

Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase

2005

Okajima, T.; Kishishita, S.; Chiu, Y.C.; Murakawa, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Kuroda, S.; Tanizawa, K.

Biochemistry

44

12041-12048

672146

16566584

Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase

2006

Chiu, Y.C.; Okajima, T.; Murakawa, T.; Uchida, M.; Taki, M.; Hirota, S.; Kim, M.; Yamaguchi, H.; Kawano, Y.; Kamiya, N.; Kuroda, S.; Hayashi, H.; Yamamoto, Y.; Tanizawa, K.

Biochemistry

45

4105-4120

672153

16605246

Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins

2006

Li, M.; Binda, C.; Mattevi, A.; Edmondson, D.E.

Biochemistry

45

4775-4784

672200

16846222

A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction

2006

Juda, G.A.; Shepard, E.M.; Elmore, B.O.; Dooley, D.M.

Biochemistry

45

8788-8800

672492

17142964

Substrate selectivity of monoamine oxidase A, monoamine oxidase B, diamine oxidase, and semicarbazide-sensitive amine oxidase in COS-1 expression systems

2006

Ochiai, Y.; Itoh, K.; Sakurai, E.; Adachi, M.; Tanaka, Y.

Biol. Pharm. Bull.

29

2362-2366

672525

15848762

Mutation of surface cysteine 374 to alanine in monoamine oxidase A alters substrate turnover and inactivation by cyclopropylamines

2005

Vintem, A.P.; Price, N.T.; Silverman, R.B.; Ramsay, R.R.

Bioorg. Med. Chem.

13

3487-3495

675073

16917825

Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)

2006

Anichtchik, O.; Sallinen, V.; Peitsaro, N.; Panula, P.

J. Comp. Neurol.

498

593-610

675286

15689151

Alkylamino derivatives of 4-aminomethylpyridine as inhibitors of copper-containing amine oxidases

2005

Bertini, V.; Buffoni, F.; Ignesti, G.; Picci, N.; Trombino, S.; Iemma, F.; Alfei, S.; Pocci, M.; Lucchesini, F.; De Munno, A.

J. Med. Chem.

48

664-670

676315

15922018

Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism

2005

Krueger, S.K.; Williams, D.E.

Pharmacol. Ther.

106

357-387

685188

17636875

Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase

2007

Hothi, P.; Roujeinikova, A.; Khadra, K.A.; Lee, M.; Cullis, P.; Leys, D.; Scrutton, N.S.

Biochemistry

46

9250-9259

685206

18052255

Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism

2008

Hothi, P.; Lee, M.; Cullis, P.M.; Leys, D.; Scrutton, N.S.

Biochemistry

47

183-194

685296

18512962

Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus

2008

Cavalieri, C.; Biermann, N.; Vlasie, M.D.; Einsle, O.; Merli, A.; Ferrari, D.; Rossi, G.L.; Ubbink, M.

Biochemistry

47

6560-6570

686264

18691041

Semicarbazide-sensitive amine oxidase/vascular adhesion protein 1: recent developments concerning substrates and inhibitors of a promising therapeutic target

2008

Dunkel, P.; Gelain, A.; Barlocco, D.; Haider, N.; Gyires, K.; Sperlagh, B.; Magyar, K.; Maccioni, E.; Fadda, A.; Matyus, P.

Curr. Med. Chem.

15

1827-1839

686425

18177365

Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U

2008

Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.

Environ. Microbiol.

10

413-432

687276

17715921

Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis

2007

Moore, R.H.; Spies, M.A.; Culpepper, M.B.; Murakawa, T.; Hirota, S.; Okajima, T.; Tanizawa, K.; Mure, M.

J. Am. Chem. Soc.

129

11524-11534

687589

17475620

New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates

2007

Roujeinikova, A.; Hothi, P.; Masgrau, L.; Sutcliffe, M.J.; Scrutton, N.S.; Leys, D.

J. Biol. Chem.

282

23766-23777

688193

17521737

Substrate specificity of copper-containing plant amine oxidases

2007

Pietrangeli, P.; Federico, R.; Mondovi, B.; Morpurgo, L.

J. Inorg. Biochem.

101

997-1004

688478

17393065

Kinetic properties of recombinant MAO-A on incorporation into phospholipid nanodisks

2007

Cruz, F.; Edmondson, D.E.

J. Neural Transm.

114

699-702

688481

17401534

Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-As

2007

Wang, J.; Edmondson, D.E.

J. Neural Transm.

114

721-724

688492

17823767

Differential behavioral syndrome evoked in the rats after multiple doses of SSRI fluoxetine with selective MAO inhibitors rasagiline or selegiline

2008

Speiser, Z.; Fine, T.; Litinetsky, L.; Eliash, S.; Blaugrund, E.; Cohen, S.

J. Neural Transm.

115

107-116

689175

17624626

Monoamine oxidase B activity is increased in human gliomas

2008

Gabilondo, A.M.; Hostalot, C.; Garibi, J.M.; Meana, J.J.; Callado, L.F.

Neurochem. Int.

52

230-234

696563

19182394

Phenylethylamide and phenylmethylamide derivatives as new tyrosinase inhibitors

2009

Le Mellay-Hamon, V.; Criton, M.

Biol. Pharm. Bull.

32

301-303

696719

18024134

Synthesis of 4,5,6,7-tetrahydrothieno[3,2-c]pyridines and comparison with their isosteric 1,2,3,4-tetrahydroisoquinolines as inhibitors of phenylethanolamine N-methyltransferase

2008

Grunewald, G.L.; Seim, M.R.; Bhat, S.R.; Wilson, M.E.; Criscione, K.R.

Bioorg. Med. Chem.

16

542-559

703130

19588076

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

2009

Kaitaniemi, S.; Elovaara, H.; Groen, K.; Kidron, H.; Liukkonen, J.; Salminen, T.; Salmi, M.; Jalkanen, S.; Elima, K.

Cell. Mol. Life Sci.

66

2743-2757

703627

18573102

The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex

2008

Dunn, R.V.; Marshall, K.R.; Munro, A.W.; Scrutton, N.S.

FEBS J.

275

3850-3858

703657

19645722

Mutagenic probes of the role of Ser209 on the cavity shaping loop of human monoamine oxidase A

2009

Wang, J.; Harris, J.; Mousseau, D.D.; Edmondson, D.E.

FEBS J.

276

4569-4581

705496

19789505

Monoamine oxidase and semicarbazide sensitive amine oxidase activities in normal and inflamed human dental pulp

2009

Vavilova, T.; Ostrovskaya, I.; Axenova, L.; Buneeva, O.; Medvedev, A.

Med. Sci. Monit.

15

BR289-BR292

705901

18442871

Increase of monoamine oxidase-B activity in the brain of scrapie-infected hamsters

2008

Adjou, K.T.; Dilda, P.; Aumond, P.; Gueddari, S.; Deslys, J.P.; Dormont, D.; Seman, M.

Neurochem. Int.

52

1416-1421

706602

19883764

High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparison with human MAO A

2009

Wang, J.; Edmondson, D.E.

Protein Expr. Purif.

70

211-217

706934

19198157

Comparative study of catalytic properties of mink and rat liver monoamine oxidase

2008

Iagodina, O.

Zh. Evol. Biokhim. Fiziol.

44

570-576

711407

20382016

Chromone-2- and -3-carboxylic acids inhibit differently monoamine oxidases A and B

2010

Alcaro, S.; Gaspar, A.; Ortuso, F.; Milhazes, N.; Orallo, F.; Uriarte, E.; Yanez, M.; Borges, F.

Bioorg. Med. Chem. Lett.

20

2709-2712

711832

20848919

Enzymological characteristic of monoamine oxidase from the visual ganglia of the Pacific squid Todarodes pacificus

2009

Yagodina, O.

Dokl. Biochem. Biophys.

428

284-287

711912

20702005

Synthesis of new 3-aryl-4,5-dihydropyrazole-1-carbothioamide derivatives. An investigation on their ability to inhibit monoamine oxidase

2010

Maccioni, E.; Alcaro, S.; Orallo, F.; Cardia, M.C.; Distinto, S.; Costa, G.; Yanez, M.; Sanna, M.L.; Vigo, S.; Meleddu, R.; Secci, D.

Eur. J. Med. Chem.

45

4490-4498

713457

20079438

Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B

2010

Arslan, B.K.; Edmondson, D.E.

Protein Expr. Purif.

70

290-297

719067

22579486

Acylprolinamides: A new class of peptide deformylase inhibitors with in vivo antibacterial activity

2012

Axten, J.M.; Medina, J.R.; Blackledge, C.W.; Duquenne, C.; Grant, S.W.; Bobko, M.A.; Peng, T.; Miller, W.H.; Pinckney, T.; Gallagher, T.F.; Kulkarni, S.; Lewandowski, T.; Van Aller, G.S.; Zonis, R.; Ward, P.; Campobasso, N.

Bioorg. Med. Chem. Lett.

22

4028-4032

720287

21643793

An improved approach to steady-state analysis of monoamine oxidases

2011

Ramsay, R.R.; Olivieri, A.; Holt, A.

J. Neural Transm.

118

1003-1019

720470

22998157

Functional diversity of Teleost arylalkylamine N-acetyltransferase-2: is the timezyme evolution driven by habitat temperature?

2012

Cazamea-Catalan, D.; Magnanou, E.; Helland, R.; Vanegas, G.; Besseau, L.; Boeuf, G.; Paulin, C.H.; Joergensen, E.H.; Falcon, J.

Mol. Ecol.

21

5027-5041

720626

20832472

On the formation and nature of the imidazoline I2 binding site on human monoamine oxidase-B

2010

McDonald, G.R.; Olivieri, A.; Ramsay, R.R.;, Holt, A.

Pharmacol. Res.

62

475-488

720789

21424826

Substrate promiscuity of a rosmarinic acid synthase from lavender (Lavandula angustifolia L.)

2011

Landmann, C.; Huecherig, S.; Fink, B.; Hoffmann, T.; Dittlein, D.; Coiner, H.A.; Schwab, W.

Planta

234

305-320

720933

22753468

Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti

2012

Han, Q.; Robinson, H.; Ding, H.; Christensen, B.M.; Li, J.

Proc. Natl. Acad. Sci. USA

109

11669-11674

723891

-

Purification and characterisation of monoamine oxidase from Avena sativa

2012

Zhang, Y.; Livingstone, J.; Hirasawa, E.

Acta Physiol. Plant.

34

1411-1419

723927

21644017

Characterization and application of a diamine oxidase from Lathyrus sativus as component of an electrochemical biosensor for the determination of biogenic amines in wine and beer

2011

Di Fusco, M.; Federico, R.; Boffi, A.; Macone, A.; Favero, G.; Mazzei, F.

Anal. Bioanal. Chem.

401

707-716

724280

20052994

Exploring the roles of the metal ions in Escherichia coli copper amine oxidase

2010

Smith, M.A.; Pirrat, P.; Pearson, A.R.; Kurtis, C.R.; Trinh, C.H.; Gaule, T.G.; Knowles, P.F.; Phillips, S.E.; McPherson, M.J.

Biochemistry

49

1268-1280

724322

21585208

Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3

2011

Elovaara, H.; Kidron, H.; Parkash, V.; Nymalm, Y.; Bligt, E.; Ollikka, P.; Smith, D.; Pihlavisto, M.; Salmi, M.; Jalkanen, S.; Salminen, T.

Biochemistry

50

5507-5520

724603

23924738

Purification and molecular analysis of a monoamine oxidase isolated from Narcissus tazetta

2013

Cui, Z.; Zhang, Y.; Inoue, H.; Yogo, S.; Hirasawa, E.

Biosci. Biotechnol. Biochem.

77

1728-1733

724966

21978362

The gating residues Ile199 and Tyr326 in human monoamine oxidase B function in substrate and inhibitor recognition

2011

Milczek, E.M.; Binda, C.; Rovida, S.; Mattevi, A.; Edmondson, D.E.

FEBS J.

278

4860-4869

725314

21984603

Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors

2012

Murakawa, T.; Hayashi, H.; Taki, M.; Yamamoto, Y.; Kawano, Y.; Tanizawa, K.; Okajima, T.

J. Biochem.

151

167-178

725620

-

Catalytic characteristics of monoamine oxidase of whitefish Coregonus lavaretus ludoga

2011

Basova, I.; Yagodina, O.

J. Evol. Biochem. Physiol.

47

321-327

725621

-

Reactivity of liver monoamine oxidase in the seal Phoca hispida ladogensis

2013

Basova, I.; Yagodina, O.

J. Evol. Biochem. Physiol.

49

138-144

725622

-

Liver monoamine oxidase activity of the lamprey Lampetra fluviatilis. The substrate-inhibitor specificity

2013

Yagodina, O.; Basova, I.

J. Evol. Biochem. Physiol.

49

53-58

725733

-

Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus

2012

Foster, A.; Barnes, N.; Speight, R.; Keane, M.

J. Mol. Catal. B

74

73-82

725736

-

Expression of rat diamine oxidase in Escherichia coli

2012

Rosini, E.; Nossa, S.; Valentino, M.; DArrigo, P.; Marinesco, S.; Pollegioni, L.

J. Mol. Catal. B

82

115-120

726290

22238597

Implication for functions of the ectopic adipocyte copper amine oxidase (AOC3) from purified enzyme and cell-based kinetic studies

2012

Shen, S.H.; Wertz, D.L.; Klinman, J.P.

PLoS ONE

7

e29270

726378

21383134

Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family

2011

Kachalova, G.; Decker, K.; Holt, A.; Bartunik, H.D.

Proc. Natl. Acad. Sci. USA

108

4800-4805

726536

23225177

Characterization of amine oxidases from Arthrobacter aurescens and application for determination of biogenic amines

2013

Lee, J.I.; Kim, Y.W.

World J. Microbiol. Biotechnol.

29

673-682

733172

24123742

A new synthetic route to N-benzyl carboxamides through the reverse reaction of N-substituted formamide deformylase

2014

Hashimoto, Y.; Sakashita, T.; Fukatsu, H.; Sato, H.; Kobayashi, M.

Appl. Environ. Microbiol.

80

61-69

735681

25406072

Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases

2014

Dempsey, D.R.; Jeffries, K.A.; Bond, J.D.; Carpenter, A.M.; Rodriguez-Ospina, S.; Breydo, L.; Caswell, K.K.; Merkler, D.J.

Biochemistry

53

7777-7793

735933

25912923

A novel, colorimetric method for biogenic amine detection based on arylalkylamine N-acetyltransferase

2015

Leng, P.Q.; Zhao, F.L.; Yin, B.C.; Ye, B.C.

Chem. Commun. (Camb. )

51

8712-8714

736685

26267754

Subfunctionalization of arylalkylamine N-acetyltransferases in the sea bass Dicentrarchus labrax: two-ones for one two

2015

Paulin, C.H.; Cazamea-Catalan, D.; Zilberman-Peled, B.; Herrera-Perez, P.; Sauzet, S.; Magnanou, E.; Fuentes, M.; Gothilf, Y.; Munoz-Cueto, J.A.; Falcon, J.; Besseau, L.

J. Pineal Res.

59

354-364

741494

28435530

Small molecule lysyl oxidase-like 2 (LOXL2) inhibitors the identification of an inhibitor selective for LOXL2 over LOX

2017

Hutchinson, J.H.; Rowbottom, M.W.; Lonergan, D.; Darlington, J.; Prodanovich, P.; King, C.D.; Evans, J.F.; Bain, G.

ACS Med. Chem. Lett.

8

423-427

742881

26269595

probing the catalytic mechanism of copper amine oxidase from Arthrobacter globiformis with halide ions

2015

Murakawa, T.; Hamaguchi, A.; Nakanishi, S.; Kataoka, M.; Nakai, T.; Kawano, Y.; Yamaguchi, H.; Hayashi, H.; Tanizawa, K.; Okajima, T.

J. Biol. Chem.

290

23094-23109

742933

25468423

Characterization of two amine oxidases from Aspergillus carbonarius AIU 205

2015

Sugawara, A.; Matsui, D.; Yamada, M.; Asano, Y.; Isobe, K.

J. Biosci. Bioeng.

119

629-635

742988

-

Comparative enzymologic study of catalytical properties of liver monoamine oxidases of sturgeon fish

2013

Yagodina, O.; Basova, I.

J. Evol. Biochem. Physiol.

49

300-308

742989

-

Enzymologic characteristics of monoamine oxidase from liver of the skipjack tuna Katsuwonus pelamis

2013

Basova, I.; Yagodina, O.

J. Evol. Biochem. Physiol.

49

562-569

742990

-

Catalytic properties of liver monoamine oxidase in the chum salmon Oncorhynchus keta

2015

Basova, I.; Basova, N.; Yagodina, O.

J. Evol. Biochem. Physiol.

51

370-377

743371

-

Characterization of the copper-containing amine oxidase from Trifolium pratense seedlings

2016

Zhang, Y.; Li, G.; Zhong, R.; Ma, Y.; Gong, P.; Zhang, F.

Nucl. Sci. Tech.

27

69

743457

25378687

Apple fruit copper amine oxidase isoforms peroxisomal MdAO1 prefers diamines as substrates, whereas extracellular MdAO2 exclusively utilizes monoamines

2015

Zarei, A.; Trobacher, C.P.; Cooke, A.R.; Meyers, A.J.; Hall, J.C.; Shelp, B.J.

Plant Cell Physiol.

56

137-147

743594

26556595

Primary amine oxidase of Escherichia coli is a metabolic enzyme that can use a human leukocyte molecule as a substrate

2015

Elovaara, H.; Huusko, T.; Maksimow, M.; Elima, K.; Yegutkin, G.G.; Skurnik, M.; Dobrindt, U.; Siitonen, A.; McPherson, M.J.; Salmi, M.; Jalkanen, S.

PLoS ONE

10

e0142367

743978

-

Inhibition of aromatic L-amino acid decarboxylase from Micrococcus percitreus by substrate analogs

1987

Nakazawa, H.

Agric. Biol. Chem.

51

2531-2537

753557

31162815

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

2019

Palacio, C.M.; Rozeboom, H.J.; Lanfranchi, E.; Meng, Q.; Otzen, M.; Janssen, D.B.

FEBS J.

286

4086-4102

758432

29402941

Eis, a novel family of arylalkylamine N-acetyltransferase (EC 2.3.1.87)

2018

Pan, Q.; Zhao, F.; Ye, B.

Sci. Rep.

8

2435

763366

-

Determining a novel NAD+-dependent amine dehydrogenase with a broad substrate range from Streptomyces Íirginiae IFO 12827 purification and characterization

2000

Itoh, N.; Yachi, C.; Kudome, T.

J. Mol. Catal. B

10

281-290