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• • Molecular Structure
  • Sum Formula
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• • In Vivo Substrate
  • In Vivo Product
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  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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Ligand cadaverine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

lysine metabolism

KEGG

Biosynthesis of alkaloids derived from ornithine, lysine and nicotinic acid, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Glutathione metabolism, Lysine degradation, Microbial metabolism in diverse environments, Protein digestion and absorption, Tropane, piperidine and pyridine alkaloid biosynthesis more

MetaCyc

aminopropylcadaverine biosynthesis, bisucaberin biosynthesis, cadaverine biosynthesis, desferrioxamine B biosynthesis, desferrioxamine E biosynthesis, L-lysine degradation I, L-lysine degradation X, lupanine biosynthesis more

Show all BRENDA pathways known for cadaverine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + cadaverine = 5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine

719710

-

2.6.1.113

cadaverine + pyruvate = 1-aminopentane + alanine

739832

-

2.6.1.29

cadaverine + 2-oxoglutarate = 5-aminopentanal + L-glutamate

639953

-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.62

acetylcadaverine + H2O = acetate + cadaverine

-

-

4.1.1.17

L-lysine = 1,5-diaminopentane + CO2

649722

2oo0, 3D-view

4.1.1.18

L-Lys = Cadaverine + CO2

-

5gjp, 3D-view

4.1.1.18

L-lysine = cadaverine + CO2

-

5gjp, 3D-view

4.1.1.18

2 entries

4.1.1.B12

L-lysine = cadaverine + CO2

-

-

Substrate in Enzyme-catalyzed Reactions (64 results)

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Show Substrate (64 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.59

1,5-Diaminopentane + NADPH + O2 = ?

207904

-

1.4.3.10

cadaverine + O2 + H2O = 5-aminopentanal + NH3 + H2O2

395442, 395437, 395440, 395447, 288077, 395444, 684634, 724877, 725184

-

1.4.3.13

1,5-diaminopentane + O2 + H2O = ?

742424

-

1.4.3.13

1,5-diaminopentane + O2 + H2O = ? + NH3 + H2O2

689199

-

1.4.3.13

cadaverine + O2 + H2O = ?

675900, 671973

-

1.4.3.21

1,5-diaminopentane + H2O + O2 = ?

742933

-

1.4.3.21

cadaverine + H2O + O2 = ?

743371, 726536

-

1.4.3.21

cadaverine + H2O + O2 = DELTA1-piperideine + NH3 + H2O2

724537

-

1.4.3.22

1,5-diaminopentane + H2O + O2 = 5-aminopentanal + NH3 + H2O2

391940, 391941, 391922, 391920, 391952, 391953, 391959, 391925, 391945, 391943, 391954, 391935, 391947, 391926

-

1.4.3.22

cadaverine + H2O + O2 = 5-aminopentanal + NH3 + H2O2

704175, 689424, 391948, 723927, 391927, 347973, 720756

-

1.4.3.22

cadaverine + H2O + O2 = ?

656295, 686129, 686654, 672497, 742417, 655478

-

1.4.3.22

cadaverine + H2O + O2 = ? + NH3 + H2O2

688193

-

1.4.3.13

3 entries

1.4.3.21

3 entries

1.4.3.22

4 entries

1.4.9.2

cadaverine + H2O + 2,6-dichlorophenol indophenol = ? + NH3 + reduced 2,6-dichlorophenol indophenol

655062

-

2.1.3.6

carbamoyl phosphate + cadaverine = phosphate + N-carbamoylcadaverine

485950, 485953, 674316

-

2.3.1.138

caffeoyl-CoA + cadaverine = CoA + N-caffeoylcadaverine

486313, 486314, 486315, 486312

-

2.3.1.48

acetyl-CoA + 1,5-pentanediamine = ?

487064

-

2.3.1.57

acetyl-CoA + 1,5-diaminopentane = CoA + N1-acetyl-1,5-diaminopentane

487257, 487256, 487260, 487259

-

2.3.2.13

N-carbobenzoxy-Gln-Gly + cadaverine = ?

736480

-

2.3.2.13

Z-Gln-Gly + cadaverine = ?

735541

-

2.3.2.13

2 entries

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + cadaverine = 5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine

719710, 719718

-

2.5.1.16

S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane = 5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane

639706, 639707, 392545, 489861, 489867, 639705, 639709, 639718, 639697

-

2.5.1.44

putrescine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane

288702, 288699

-

2.5.1.44

spermidine + cadaverine = (4-aminobutyl)(5-aminopentyl)amine + sym-homospermidine + propane-1,3-diamine + putrescine

739672

-

2.5.1.44

spermidine + cadaverine = homospermidine + N-(4-aminobutyl)-1,5-diaminopentane

288699, 288702

-

2.5.1.44

3 entries

2.6.1.113

cadaverine + pyruvate = 1-aminopentane + alanine

739832

-

2.6.1.18

cadaverine + propionaldehyde = ? + 1-aminopropane

737507

-

2.6.1.19

cadaverine + 2-oxoglutarate = L-glutamate + 5-aminopentanal

661969

-

2.6.1.19

cadaverine + 2-oxoglutarate = L-glutamate + ?

637056

-

2.6.1.19

2 entries

2.6.1.29

cadaverine + 2-oxoglutarate = 5-aminopentanal + L-glutamate

639953, 639950, 639951

-

2.6.1.82

13,5-dimethoxybenzaldehyde + cadaverine = 2,3-dimethoxybenzylamine + piperideine + H2O

759219

-

2.6.1.82

1H-indole-2-carbaldehyde + cadaverine = 1-(1H-indol-2-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

2,3-dimethoxybenzaldehyde + cadaverine = 3,5-dimethoxybenzylamine + piperideine + H2O

759219

-

2.6.1.82

2,4-dimethoxybenzaldehyde + cadaverine = 2,4-dimethoxybenzylamine + piperideine + H2O

759219

-

2.6.1.82

2-(trifluoromethyl)benzaldehyde + cadaverine = 2-(trifluoromethyl)benzylamine + piperideine + H2O

759219

-

2.6.1.82

2-formylbenzoic acid + cadaverine = 2-(aminomethyl)benzoic acid + piperideine + H2O

759219

-

2.6.1.82

2-formylbenzonitrile + cadaverine = 2-(aminomethyl)benzonitrile + piperideine + H2O

759219

-

2.6.1.82

2-methoxybenzaldehyde + cadaverine = 2-methoxybenzylamine + piperideine + H2O

759219

-

2.6.1.82

2-methoxypyridine-3-carbaldehyde + cadaverine = 1-(2-methoxypyridin-3-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

2H-1,3-benzodioxole-4-carbaldehyde + cadaverine = 1-(2H-1,3-benzodioxol-4-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

3,4-difluorobenzaldehyde + cadaverine = 3,4-difluorobenzylamine + piperideine + H2O

759219

-

2.6.1.82

3,5-dibromobenzaldehyde + cadaverine = 3,5-dibromobenzylamine + piperideine + H2O

759219

-

2.6.1.82

3-acetylbenzoic acid + cadaverine = 3-(1-aminoethyl)benzoic acid + piperideine + H2O

759219

-

2.6.1.82

3-chlorobenzaldehyde + cadaverine = 3-chlorobenzylamine + piperideine + H2O

759219

-

2.6.1.82

3-fluorobenzaldehyde + cadaverine = 3-fluorobenzylamine + piperideine + H2O

759219

-

2.6.1.82

3-formylbenzonitrile + cadaverine = 3-(aminomethyl)benzonitrile + piperideine + H2O

759219

-

2.6.1.82

3-methoxybenzaldehyde + cadaverine = 3-methoxybenzylamine + piperideine + H2O

759219

-

2.6.1.82

3-nitrobenzaldehyde + cadaverine = 3-nitrobenzylamine + piperideine + H2O

759219

-

2.6.1.82

4-acetylbenzoic acid + cadaverine = 4-(1-aminoethyl)benzoic acid + piperideine + H2O

759219

-

2.6.1.82

4-chlorobenzaldehyde + cadaverine = 4-chlorobenzylamine + piperideine + H2O

759219

-

2.6.1.82

4-fluorobenzaldehyde + cadaverine = 4-fluorobenzylamine + piperideine + H2O

759219

-

2.6.1.82

4-formylbenzoic acid + cadaverine = 4-(aminomethyl)benzoic acid + piperideine + H2O

759219

-

2.6.1.82

4-formylbenzonitrile + cadaverine = 4-(aminomethyl)benzonitrile + piperideine + H2O

759219

-

2.6.1.82

4-nitrobenzaldehyde + cadaverine = 4-nitrobenzylamine + piperideine + H2O

759219

-

2.6.1.82

5-chlorothiophene-2-carbaldehyde + cadaverine = 1-(5-chlorothiophen-2-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

5-formylthiophene-2-carboxylic acid + cadaverine = 5-(aminomethyl)thiophene-2-carboxylic acid + piperideine + H2O

759219

-

2.6.1.82

5-methylfuran-2-carbaldehyde + cadaverine = 1-(5-methylfuran-2-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

6-acetylpyridine-2-carboxylic acid + cadaverine = 6-(1-aminoethyl)pyridine-2-carboxylic acid + piperideine + H2O

759219

-

2.6.1.82

6-methoxypyridine-3-carbaldehyde + cadaverine = 1-(6-methoxypyridin-3-yl)methanamine + piperideine + H2O

759219

-

2.6.1.82

cadaverine + 2-oxoglutarate = L-glutamate + 5-aminopentanal

661399

-

2.6.1.82

cadaverine + 2-oxoglutarate = piperideine + L-glutamate + H2O

759219

-

2.6.1.82

quinoline-3-carbaldehyde + cadaverine = 1-(quinolin-3-yl)methanamine + piperideine + H2O

759219

-

2.6.1.B22

1-phenylpentane-2,4-dione + cadaverine = ?

759321

-

2.6.1.B22

4-phenylbutan-2-one + cadaverine = ?

759321

-

2.6.1.B22

benzaldehyde + cadaverine = ?

759321

-

2.6.1.82

32 entries

2.6.1.B22

3 entries

Product in Enzyme-catalyzed Reactions (18 results)

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Show Product (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.4

acetylcadaverine + H2O = acetate + cadaverine

-

-

3.5.1.48

acetylcadaverine + H2O = acetate + cadaverine

-

-

3.5.1.53

N-carbamoylcadaverine + H2O = cadaverine + CO2 + NH3

653166

-

3.5.1.53

N-carbamoyldiaminopentane + H2O = CO2 + NH3 + diaminopentane

209192

-

3.5.1.53

2 entries

3.5.1.62

acetylcadaverine + H2O = acetate + cadaverine

-

-

3.5.3.20

1-amino-5-guanidinopentane + H2O = 1,5-diaminopentane + urea

-

-

4.1.1.116

D-lysine = cadaverine + CO2

-

-

4.1.1.17

L-Lys = 1,5-diaminopentane + CO2

-

2oo0, 3D-view

4.1.1.17

L-lysine = 1,5-diaminopentane + CO2

649722,

2oo0, 3D-view

4.1.1.17

L-lysine = cadaverine + CO2

-

2oo0, 3D-view

4.1.1.18

L-lysine = 1,5-diaminopentane + CO2

-

5gjp, 3D-view

4.1.1.18

L-Lys = Cadaverine + CO2

, 37288, 37286, 37289, 37292, 37293, 37299, 37297, 37294, 37295, 37296, 37298, 37290, 37283, 37285, 37300, 37284, 37287, 37291

5gjp, 3D-view

4.1.1.18

L-lysine = cadaverine + CO2

-

5gjp, 3D-view

4.1.1.17

3 entries

4.1.1.18

3 entries

4.1.1.19

L-lysine = 1,5-diaminopentane + CO2

-

-

4.1.1.57

L-norleucine = pentane-1,5-diamine + CO2

-

-

4.1.1.86

L-lysine = 1,5-diaminopentane + CO2

-

-

4.1.1.B12

D-lysine = cadaverine + CO2

-

-

4.1.1.B12

L-lysine = cadaverine + CO2

-

-

4.1.1.B12

2 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.13

up to 40% stimulation at 1 mm

441207

-

3.1.13.1

can replace missing Mg2+ to a small extent

134049

-

4.1.1.50

57% of activation by putrescine

650473

-

4.1.1.50

stimulates

4676

-

4.1.1.50

activates

4668, 4676

-

4.1.1.50

increase of kcat up to 9fold

653168

-

4.1.1.50

4 entries

Inhibitor in Enzyme-catalyzed Reactions (43 results)

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Show Inhibitors (43 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.99.29

87% of initial activity at 0.5 mM

438288

-

1.4.1.B4

10 mM, causes 10-20% inhibition of carboxynorspermidine formation

712623

-

1.4.3.10

noncompetitive against putrescine

395438

-

1.4.3.14

24% inhibition

391751

-

1.4.3.20

0.2 mM, 74% inhibition

672432

-

1.5.1.3

12 mM

392238

-

1.5.1.8

3 mM, 26% loss of activity

392361

-

1.5.3.14

-

654744

-

2.1.1.53

-

485445, 706130

-

2.1.1.53

strong inhibitor

676699

-

2.1.1.53

2 entries

2.3.1.1

10 mM, 80% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate

486069

-

2.3.1.57

30% inhibition

487261

-

2.3.2.13

2 mM, 70% inhibition

658929

-

2.3.2.13

complete inhibition at 0.15 mM

719249

-

2.3.2.13

strong, putrescine as substrate

487854

-

2.5.1.16

weak, competitive

639709

-

2.5.1.16

-

489867

-

2.5.1.16

26-39% inhibition

639697

-

2.5.1.16

77% inhibition at 0.01 mM and 22% inhibition at 1 mM

639710

-

2.5.1.16

weak

639700

-

2.5.1.44

weak inhibition

288697

-

2.5.1.44

-

288698

-

2.3.2.13

3 entries

2.5.1.16

5 entries

2.5.1.44

2 entries

2.5.1.45

mixed type inhibition

638089

-

2.6.1.13

-

637098

-

2.6.1.13

fully reversed by addition of pyridoxal phosphate, 57% inhibition at 10 mM after 20 min

637121

-

2.6.1.13

2 entries

2.6.1.43

14% inhibition

640045

-

2.7.1.35

-

641409

-

2.7.7.48

-

643354

-

3.5.1.48

cadaverine; Ki: 1.5 mM

172053

-

3.5.3.12

-

209398, 209402

-

3.5.3.12

competitive inhibition

209397

-

3.7.1.3

-

289268

-

3.7.1.3

competitive inhibition, 10 mM

289258

-

4.1.1.17

-

4000

2oo0, 3D-view

4.1.1.17

1 mM, 46% inhibition

651824

2oo0, 3D-view

4.1.1.18

-

715142

5gjp, 3D-view

4.1.1.18

-

37297

5gjp, 3D-view

4.1.1.18

competitive inhibition mechanism, 90% inhibition at 10 mM

748418

5gjp, 3D-view

3.5.3.12

2 entries

3.7.1.3

2 entries

4.1.1.17

2 entries

4.1.1.18

3 entries

4.1.1.19

-

4101

-

4.1.1.20

-

653897

-

6.1.1.6

-

652528

-

6.1.1.6

ATP-diphosphate exchange reaction

479

-

6.1.1.6

2 entries

6.3.4.19

-

704642

-

3D Structure of Enzyme-Ligand-Complex (PDB) (7 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (7 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.1

3qj5, 3D-view

1.1.1.284

3qj5, 3D-view

2.7.11.12

4ofg, 3D-view

2.7.7.60

1h3m, 3D-view

4.1.1.17

2oo0, 3D-view

4.1.1.18

5gjp, 3D-view

4.3.2.2

4nsl, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (12 results)

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Show Turnover Number (12 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.10

1.72

-

at pH 8.0 and 55°C

725184

1.4.3.10

3.9

-

wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

684634

1.4.3.21

0.0619

-

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

726536

1.4.3.21

1

-

in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

724537

1.4.3.22

0.9

-

xenon-treated enzyme

686654

1.4.3.22

4.5

-

-

686654

1.4.3.22

72.8

-

pH 8.5, 25°C

688193

1.4.3.22

159

-

pH 7.2, 25°C

655478, 688193

1.4.3.22

498

-

-

391948

1.4.3.22

27180

-

pH 7.2, 37°C

656295

2.5.1.104

0.02

-

pH 9.0, 70°C

719718

2.5.1.104

2.09

-

pH 7.4, 70°C

719710

1.4.3.10

2 entries

1.4.3.21

2 entries

1.4.3.22

6 entries

2.5.1.104

2 entries

K_M Value (37 results)

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Show KM Value (37 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.10

0.018

-

wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

684634

1.4.3.10

0.36

-

at pH 8.0 and 55°C

725184

1.4.3.10

1.1

-

-

395444

1.4.3.21

0.089

-

at pH 7.0 and 37°C

743371

1.4.3.21

0.3

-

in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

724537

1.4.3.21

12.7

-

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

726536

1.4.3.22

0.0146

-

-

391945

1.4.3.22

0.019

-

-

391927

1.4.3.22

0.0279

-

-

391947

1.4.3.22

0.03

-

pH 7.2, 37°C

656295

1.4.3.22

0.06

-

pH 8.5, 25°C

688193

1.4.3.22

0.065

-

-

391948

1.4.3.22

0.09

-

-

391954

1.4.3.22

0.1

-

-

686654

1.4.3.22

0.1

-

pH 7.2, 25°C

688193

1.4.3.22

0.13

-

-

391959

1.4.3.22

0.172

-

free enzyme, in 0.1 M phosphate buffer, pH 7.4, at 25°C

723927

1.4.3.22

0.21

-

-

391943

1.4.3.22

0.23

-

xenon-treated enzyme

686654

1.4.3.22

0.26

-

pH 7.9, 30°C, lowest KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 96.2 pkat

720756

1.4.3.22

0.3

-

pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 20.5 pkat

720756

1.4.3.22

0.4

-

-

391925

1.4.3.22

0.47

-

-

391935

1.4.3.22

0.47

-

-

391935

1.4.3.22

0.73

-

at pH 7.4

391918

1.4.3.22

0.83

-

at pH 8.5

391918

1.4.3.22

1.3

-

at pH 6.3

391918

1.4.3.22

1.79

-

Vmax: 5.2 nkat, pH and temperature not specified in the publication

689424

1.4.3.22

2.6

-

free enzyme

391920

1.4.3.22

2.84

-

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

723927

1.4.3.22

6.25

-

pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 19.6 pkat, specifiity constant 1% of the constant for N-methylputrescine

720756

1.4.3.22

8.1

-

immobilized enzyme

391920

1.4.3.10

3 entries

1.4.3.21

3 entries

1.4.3.22

26 entries

2.1.3.6

7.7

-

-

485953

2.3.1.57

0.1

-

-

487257

2.3.1.57

0.44

-

-

487256

2.5.1.104

0.0807

-

pH 9.0, 70°C

719718

2.5.1.104

3.77

-

pH 7.4, 70°C

719710

2.3.1.57

2 entries

2.5.1.104

2 entries

K_i Value (7 results)

top print hide

Show KI Value (7 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.10

0.28

-

-

395438

1.5.3.14

0.038

-

pH 6.0, 25°C

654744

2.1.1.53

0.04

-

-

485445

2.5.1.45

0.058

-

-

638089

3.5.1.48

1.5

-

-

172053

4.1.1.18

0.46

-

recombinant enzyme, pH 7.5, 37°C

748418

4.1.1.20

0.004

-

-

653897

IC₅₀ Value (1 result)

top print hide

Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

6.3.4.19

0.91

-

pH 8.5, 21°C

704642

References & Links

Literature References (154)

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Show Reference (154 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

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1984

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1983

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37289

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1983

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37290

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1983

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37291

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1974

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37293

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1974

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Biochemistry

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37294

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37295

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Crystalline lysine decarboxylase

1969

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Studies of enzyme-mediated reactions. Part 14. Stereochemical course of the formation of cadaverine by decarboxylation of (2S)-lysine with lysine decarboxylase (E.C. 4.1.1.18) from Bacillus cadaveris

1982

Battersby, A.R.; Murphy, R.; Staunton, J.

J. Chem. Soc. Perkin Trans. I

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37297

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Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus

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239

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172053

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207904

2518519

Isolation and some properties of lysine N6-hydroxylase from Escherichia coli strain EN222

1989

Plattner, H.J.; Pfefferle, P.; Romaguera, A.; Waschutza, S.; Dieckman, H.

Biol. Met.

2

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209192

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Substrate utilization by grape N-carbamoylputrescine amidohydrolase: the final enzyme in putrescine biosynthesis

1997

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48

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209397

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Purification and properties of agmatine iminohydrolase from groundnut cotyledons

1979

Sindhu, R.K.; Desai, H.V.

Phytochemistry

18

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Corn agmatine iminohydrolase. Purification and properties

1981

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Agmatine deiminase in rice seedlings

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Specific measurement of putrescine with putrescine oxidase and aminobutyraldehyde dehydrogenase

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1953

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Phytochemistry

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391751

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L-Lysine alpha-oxidase from Trichoderma viride i4. Purification and characterization

1994

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On the active site of diamine oxidase: kinetic studies

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Characterization of free and immobilized amine oxidases

1989

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11

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391922

6403048

Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism

1983

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391925

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Diamine oxidase from Lens esculenta seedlings: purification and properties

1983

Floris, G.; Giartosio, A.; Rinaldi, A.

Phytochemistry

22

1871-1874

391926

-

Purification and characterization of diamine oxidase from rice embryos

1984

Chaudhuri, M.M.; Ghosh, B.

Phytochemistry

23

241-243

391927

-

Purification and characterization of diamine oxidase from clover leaves

1987

Delhaize, E.; Webb, J.

Phytochemistry

26

641-643

391935

6814913

Purification and properties of diamine oxidase from Euphorbia latex

1982

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Eur. J. Biochem.

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391940

2798365

Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: purification and properties

1989

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Prep. Biochem.

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391941

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Purification and properties of the diamine oxidase from Vicia faba leaves

1981

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22

737-746

391943

-

Diamine oxidase from sainfon (Onobrychis viciifolia). Purification and some properties

1989

Pec, P.; Zajoncova, L.; Jilek, M.

Biologia (Bratisl. )

44

1177-1184

391945

-

Lentil seedlings amine oxidase: preparation and properties of the copper-free enzyme

1986

Matsumiya, M.; Otake, S.

Nippon Suisan Gakkaishi

52

1617-1623

391947

-

Purification and properties of diamine oxidase from human kidney

1987

Suzuki, O.; Matsumoto, T.

Biogenic Amines

4

237-245

391948

8239662

Purification and characterization of amine oxidase from soybean seedlings

1993

Vianello, F.; Di Paolo, M.L.; Stevanato, R.; Gasparini, R.; Rigo, A.

Arch. Biochem. Biophys.

307

35-39

391952

-

Purification and characterization of diamine oxidase from Triticum aestivum shoots

1996

Suzuki, Y.

Phytochemistry

42

291-293

391953

8620882

Two distinct quinoprotein amine oxidases are induced by n-butylamine in the mycelia of Aspergillus niger AKU 3302. Purification, characterization, cDNA cloning and sequencing

1996

Frebort, I.; Tamaki, H.; Ishida, H.; Pec, P.; Luhova, L.; Tsuno, H.; Halata, M.; Asano, Y.; Kato, Y.; et al.

Eur. J. Biochem.

237

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391954

-

Quinoprotein amine oxidase from sainfoin seedlings

1997

Zajoncova, L.; Sebela, M.; Frebort, I.; Faulhammer, H.G.; Navratil, M.; Pec, P.

Phytochemistry

45

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391959

-

Analysis of the active sites of copper/topa quinone-containing amine oxidases from Lathyrus odoratus and L. sativus seedlings

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9

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392238

46

Purification and properties of Escherichia coli dihydrofolate reductase

1975

Baccanari, D.; Phillips, A.; Smith, S.; Sinski, D.; Burchall, J.

Biochemistry

14

5267-5273

392361

235294

Lysine-ketoglutarate reductase in human tissues

1975

Hutzler, J.; Dancis, J.

Biochim. Biophys. Acta

377

42-51

392545

4628436

Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines

1972

Tabor, H.; Tabor, C.W.

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203-268

395437

-

Putrescine oxidase (Micrococcus rubens)

1971

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Methods Enzymol.

17B

726-730

395438

4341347

Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme

1972

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395440

-

Role of putrescine oxidase in the generation of hydrogen peroxide by Micrococcus luteus

1985

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31

435-440

395442

7092834

Polyamine degradation in foetal and adult bovine serum

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395444

10390812

Partial purification and properties of putrescine oxidase from Candida guilliermondii

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395447

1260033

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

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Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide

1989

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441207

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Stimulation in vitro of vitamin B12-dependent methionine synthase by polyamines

1996

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316

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485445

-

Purification and properties of putrescine N-methyltransferase from transformed roots of Datura stramonium L

1994

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Planta

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485950

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Putrescine carbamoyltransferase (Streptococcus faecalis)

1983

Stalon, V.

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339343

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116850

Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis

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486069

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Separation of putrescine and spermidine hydroxycinnamoyl transferases extracted from tobacco callus

1991

Negrel, J.; Javelle, F.; Paynot, M.

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30

1089-1092

486313

16668786

Purification and properties of putrescine hydroxycinnamoyl transferase from tobacco (Nicotiana tabaccum) cell suspensions

1992

Negrel, J.; Paynot, M.; Javelle, F.

Plant Physiol.

98

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486314

16666570

Hydroxycinnamoyl-CoA:putrescine hydroxycinnamoyltransferase in tobacco cell cultures with high and low levels of caffeoylputrescine

1989

Meurer-Grimes, B.; Berlin, J.; Strack, D.

Plant Physiol.

89

488-492

486315

-

The biosynthesis of cinnamoylputrescines in callus tissue cultures of Nicotiana tabaccum

1989

Negrel, J.

Phytochemistry

28

477-481

487064

7406506

Rat liver nuclear N-acetyltransferases: separation of two enzymes with both histone and spermidine acetyltransferase activity

1980

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Arch. Biochem. Biophys.

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384-389

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

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Eur. J. Biochem.

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277-283

487257

7150547

Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver

1982

Della Ragione, F.; Pegg, A.E.

Biochemistry

21

6152-6158

487259

2775189

A novel type of putrescine (diamine)-acetylating enzyme from the nematode Ascaris suum

1989

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487260

2320051

Putrescine N-acetyltransferase in Onchocerca volvulus and Ascaris suum, an enzyme which is involved in polyamine degradation and release of N-acetylputrescine

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Mol. Biochem. Parasitol.

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487261

4841346

Acetyl-CoA:1,4-diaminobutane N-acetyltransferase. Occurence in vertebrate organs and subcellular localization

1974

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Biochim. Biophys. Acta

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487854

16665629

Evidence for transglutaminase activity in plant tissue

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Plant Physiol.

84

972-974

489861

6798961

Specificity of mammalian spermidine synthase and spermine synthase

1981

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Biochem. J.

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315-320

489867

6621389

Inhibition of aminopropyltransferases

1983

Pegg, A.E.

Methods Enzymol.

94

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637056

7362249

gamma-Aminobutyrate:alpha-ketoglutarate aminotransferase from Pseudomonas sp. F-126: purification, crystallization, and enzymologic properties

1980

Yonaha, K.; Toyama, S.

Arch. Biochem. Biophys.

200

156-164

637098

14284729

Purification and properties of rat liver ornithine DELTA-transaminase

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J. Biol. Chem.

240

1225-1230

637121

7287630

Properties of crystalline L-ornithine: alpha-ketoglutarate delta-aminotransferase from Bacillus sphaericus

1981

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J. Bacteriol.

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43-50

638089

-

Homospermidine synthase, the first pathway-specific enzyme in pyrrolizidine alkaloid biosynthesis

1993

Böttcher, F.; Adolph, R.D.; Hartmann, T.

Phytochemistry

32

679-689

639697

6743257

Polyamine synthesis in mammalian tissues. Isolation and characterization of spermidine synthase from bovine brain

1984

Raina, A.; Hyvönen, T.; Eloranta, T.; Voutilainen, M.; Samejima, K.; Yamanoha, B.

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991-1000

639700

7396502

Action of decarboxylated S-adenosylmethionine analogs in the spermidine-synthesizing system from rat prostate

1980

Samejima, K.; Nakazawa, Y.

Arch. Biochem. Biophys.

201

241-246

639705

6312269

Purification of putrescine aminopropyltransferase (spermidine synthase) from eukaryotic tissues

1983

Samejima, K.; Raina, A.; Yamanoha, B.; Eloranta, T.

Methods Enzymol.

94

270-276

639706

4572733

Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli

1973

Bowman, W.H.; White Tabor, C.; Tabor, H.

J. Biol. Chem.

248

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639707

6312268

Putrescine aminopropyltransferase (Escherichia coli)

1983

White Tabor, C.; Tabor, H.

Methods Enzymol.

94

265-270

639709

7103507

Purification of spermidine synthase from rat ventral prostate by affinity chromatography on immobilized S-adenosyl(5)-3-thiopropylamine

1982

Samejima, K.; Yamanoha, B.

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Biosynthesis of spermidine, a direct precursor of pyrrolizidine alkaloids in root cultures of Senecio vulgaris L.

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Planta

211

239-245

639718

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The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor

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Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli

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239

783-786

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Diamine-alpha-ketoglutarate aminotransferase (Escherichia coli)

1971

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Methods Enzymol.

17B

812-815

639953

2492500

Lysine catabolism in Streptomyces spp. is primarily through cadaverine: beta-lactam producers also make alpha-aminoadipate

1989

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640045

13938132

gamma, delta-Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides

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Inhibition of pyridoxal kinase from rat liver in vitro by aromatic and aliphatic amines

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Gaeng, V.; von Collins, E.N.

Int. J. Vitam. Nutr. Res.

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643354

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Activity of Foot-and-mouth disease virus RNA-dependent RNA polymerase in vitro: inhibition by polyamines and poly(amino acid)s

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