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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, D-Amino acid metabolism, 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

PAGES

479

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1996

Takita, T.; Ohkubo, Y.; Shima, H.; Muto, T.; Shimizu, N.; Sukata, H.; Ito, Y.; Saito, Y.; Inouye, K.; Hiromi, K.; Tonomura, B.

J. Biochem.

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680-689

4000

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Ornithine decarboxylase from embryos of jute seeds

1988

Pandit, M.; Ghosh, B.

Phytochemistry

27

1609-1610

4101

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Purification and partial characterization of arginine decarboxylase from Brassica campestris

1996

Das, S.; Bhaduri, T.J.; Bose, A.; Ghosh, B.

J. Plant Biochem. Biotechnol.

5

123-126

4668

6364703

Methionine adenosyltransferase (S-adenosylmethionine synthetase) and S-adenosylmethionine decarboxylase

1984

White Tabor, C.; Tabor, H.

Adv. Enzymol. Relat. Areas Mol. Biol.

56

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4676

1108876

S-Adenosylmethionine decarboxylase from baker's yeast

1975

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Biochem. J.

151

67-73

37283

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Lysine decarboxylase from Hafnia alvei: purification, molecular data and preparation of polyclonal antibodies

1987

Beier, H.; Fecker, L.F.; Berlin, J.

Z. Naturforsch. C

42

1307-1312

37284

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Lysine decarboxylase activity and alkaloid production in Heimia salicifolia cultures

1986

Pelosi, L.A.; Rother, A.; Edwards, J.M.

Phytochemistry

25

2315-2319

37285

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Cloning and characterization of a lysine decarboxylase gene from Hafnia alvei

1986

Fecker, L.F.; Beier, H.; Berlin, J.

Mol. Gen. Genet.

203

177-184

37286

3887985

Lysine decarboxylase assay by the pH-stat method

1985

Vienozinskiene, J.; Januseviciute, R.; Pauliukonis, A.; Kazlauskas, D.

Anal. Biochem.

146

180-183

37287

6439203

Inhibition of growth of Mycoplasma dispar by DL-alpha-difluoromethyllsine, a selective irreversible inhibitor of lysine decarboxylase, and reversal by cadaverine (1,5-diaminopentane)

1984

Poesoe, H.; McCann, P.P.; Tanskanen, R.; Bey, P.; Sjoerdsma, A.

Biochem. Biophys. Res. Commun.

125

205-210

37288

-

Lysine decarboxylase in plants and its integration in quinolizidine alkaloid biosynthesis

1983

Schoofs, G.; Teichmann, S.; Hartmann, T.; Wink, M.

Phytochemistry

22

65-69

37289

6353151

Lysine decarboxylase (Escherichia coli B)

1983

Boeker, E.A.; Fischer, E.H.

Methods Enzymol.

94

180-184

37290

6401702

Purification and properties of Selenomonas ruminantium lysine decarboxylase

1983

Kamio, Y.; Terawaki, Y.

J. Bacteriol.

153

658-664

37291

7389917

A chloroplast-localized lysine decarboxylase of Lupinus polyphyllus: the first enzyme in the biosynthetic pathway of quinolizidine alkaloids

1980

Hartmann, T.; Schoofs, G.; Wink, M.

FEBS Lett.

115

35-38

37292

4204273

Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5 -phosphate binding site

1974

Sabo, D.L.; Fischer, E.H.

Biochemistry

13

670-676

37293

4590109

Purification and physical properties of inducible Escherichia coli lysine decarboxylase

1974

Sabo, D.L.; Boeker, E.A.; Byers, B.; Waron, H.; Fischer, E.H.

Biochemistry

13

662-670

37294

-

L-Lysine decarboxylase (Bacterium cadaveris)

1971

Soda, K.; Moriguchi, M.

Methods Enzymol.

17B

677-681

37295

5762458

Crystalline lysine decarboxylase

1969

Soda, K.; Moriguchi, M.

Biochem. Biophys. Res. Commun.

34

34-39

37296

-

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

1982

449-453

37297

9633596

Purification and characterization of monomeric lysine decarboxylase from soybean (Glycine max) axes

1998

Kim, H.S.; Kim, B.H.; Cho, Y.D.

Arch. Biochem. Biophys.

354

40-46

37298

29123334

?-VINYLLYSINE AND ?-VINYLARGININE ARE TIME-DEPENDENT INHIBITORS OF THEIR COGNATE DECARBOXYLASES.

1996

Berkowitz, D.B.; Jahng, W.J.; Pedersen, M.L.

Bioorg. Med. Chem. Lett.

6

2151-2156

37299

9226257

Characterization of a second lysine decarboxylase isolated from Escherichia coli

1997

Kikuchi, Y.; Kojima, H.; Tanaka, T.; Takasuka, Y.; Kamio, Y.

J. Bacteriol.

179

4486-4492

37300

1799949

Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus

1991

Yamamoto, S.; Imamura, T.; Kusaba, K.; Shinoda, S.

Chem. Pharm. Bull.

39

3067-3070

134049

14257598

Purification and properties of ribonuclease II from Escherichia coli

1964

Spahr, P.F.

J. Biol. Chem.

239

3716-3726

172053

7122484

Inhibition of acetylspermidine deacetylating activity from rat liver

1982

Santacroce, M.J.; Blankenship, J.

Proc. West. Pharmacol. Soc.

25

113-118

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

1-5

209192

-

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

1997

Mendum, M.L.; Adams D.O.

Am. J. Enol. Vitic.

48

137-144

209397

-

Purification and properties of agmatine iminohydrolase from groundnut cotyledons

1979

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

Phytochemistry

18

1937-1938

209398

16661738

Corn agmatine iminohydrolase. Purification and properties

1981

Yanagisawa, H.; Suzuki, Y.

Plant Physiol.

67

697-700

209402

-

Agmatine deiminase in rice seedlings

1985

Chaudhuri, M.M.; Ghosh, B.

Phytochemistry

24

2433-2435

288077

-

Specific measurement of putrescine with putrescine oxidase and aminobutyraldehyde dehydrogenase

1988

Shimizu, E.; Tabata, Y.; Hayakawa, R.; Yorifuji, T.

Agric. Biol. Chem.

52

2865-2871

288697

437275

The formation of homospermidine by an enzyme from Rhodopseudomonas viridis

1979

Tait, G.H.

Biochem. Soc. Trans.

7

199-200

288698

7470060

Enzymic synthesis of sym-homospermidine in Lathyrus sativus (grass pea) seedlings

1980

Srivenugopal, K.S.; Adiga, P.R.

Biochem. J.

190

461-464

288699

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Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation

1994

Böttcher, F.; Ober, D.; Hartmann, T.

Can. J. Chem.

72

80-85

288702

-

Homospermidine synthase of Rhodopseudomonas viridis: substrate specificity and effects of the heterologously expressed enzyme of polyamine metabolism of Escherichia coli

1996

Ober, D.; Tholl, D.; Martin, W.; Hartmann, T.

J. Gen. Appl. Microbiol.

42

411-420

289258

13129249

Kynureninase from Neurospora: Interaction of enzyme with substrates, coenzyme, and amines

1953

Jacoby, W.B.; Bonner, D.M.

J. Biol. Chem.

205

709-715

289268

162555

Kynureninases: Enzymological properties and regulation mechanism

1979

Soda, K.; Tanizawa, K.

Adv. Enzymol. Relat. Areas Mol. Biol.

49

1-40

347973

10626376

Specificities of the enzymes of N-alkyltropane biosynthesis in Brugmansia and Datura

1999

Boswell, H.D.; Dräger, B.; McLauchlan W.R.; Portsteffen, A.; Robins D.J.; Robins R.J.; Walton, N.J.

Phytochemistry

52

871-878

391751

-

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

1994

Weber, E.; Tonder, K.; Reinbothe, C.; Unverhau, K.; Weide, H.; Aurich, H.

J. Basic Microbiol.

34

265-276

391918

5000447

On the active site of diamine oxidase: kinetic studies

1971

Costa, M.T.; Rotilio, G.; Agro, A.F.; Vallogini, M.P.; Mondovi, B.

Arch. Biochem. Biophys.

147

8-13

391920

2503012

Characterization of free and immobilized amine oxidases

1989

Stevanato, R.; Porchia, M.; Befani, O.; Mondovi, B.; Rigo, A.

Biotechnol. Appl. Biochem.

11

266-272

391922

6403048

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

1983

Bieganski, T.; Kusche, J.; Lorenz, W.; Hesterberg, R.; Stahlknecht, C.D.; Feussner, K.D.

Biochim. Biophys. Acta

756

196-203

391925

-

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

Rinaldi, A.; Floris, G.; Finazzi-Agro, A.

Eur. J. Biochem.

127

417-422

391940

2798365

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

1989

Cogoni, A.; Farci, R.; Medda, R.; Rinaldi, A.; Floris, G.

Prep. Biochem.

19

95-112

391941

-

Purification and properties of the diamine oxidase from Vicia faba leaves

1981

Matsuda, H.; Suzuki, Y.

Plant Cell Physiol.

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

255-265

391954

-

Quinoprotein amine oxidase from sainfoin seedlings

1997

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

Phytochemistry

45

239-242

391959

-

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

1998

Sebela, M.; Luhova, L.; Frebort, I.; Faulhammer, H.G.; Hirota, S.; Zajoncova, L.; Stuzka, V.; Pec, P.

Phytochem. Anal.

9

211-222

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.

Adv. Enzymol. Relat. Areas Mol. Biol.

36

203-268

395437

-

Putrescine oxidase (Micrococcus rubens)

1971

Yamada, H.

Methods Enzymol.

17B

726-730

395438

4341347

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

1972

Desa, R.J.

J. Biol. Chem.

247

5527-5534

395440

-

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

1985

Rokka, R.; Futamura, N.; Ishida, A.

J. Gen. Appl. Microbiol.

31

435-440

395442

7092834

Polyamine degradation in foetal and adult bovine serum

1982

Gahl, W.A.; Pitot, H.C.

Biochem. J.

202

603-611

395444

10390812

Partial purification and properties of putrescine oxidase from Candida guilliermondii

1999

Gunasekaran, M.; Gunasekaran, U.

Appl. Biochem. Biotechnol.

76

229-236

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

438288

2765563

Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide

1989

Abbruzzese, A.; Park, M.H.; Beninati, S.; Folk, J.E.

Biochim. Biophys. Acta

997

248-255

441207

-

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

1996

Kenyon, S.H.; Nicolaou, A.; Ast, T.; Gibbons, W.A.

Biochem. J.

316

661-665

485445

-

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

1994

Walton, N.J.; Peerless, A.C.J.; Robins, R.J.; Rhodes, M.J.C.; Boswell, H.D.; Robins, D.J.

Planta

193

9-15

485950

-

Putrescine carbamoyltransferase (Streptococcus faecalis)

1983

Stalon, V.

Methods Enzymol.

94

339343

485953

116850

Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis

1979

Wargnies, B.; Lauwers, N.; Stalon, V.

Eur. J. Biochem.

101

143-12

486069

4214023

Multiple control of N-acetylglutamate synthetase from Pseudomonas aeruginosa: synergistic inhibition by acetylglutamate and polyamines

1974

Haas, D.; Leisinger, T.

Biochem. Biophys. Res. Commun.

60

42-47

486312

-

Separation of putrescine and spermidine hydroxycinnamoyl transferases extracted from tobacco callus

1991

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

Phytochemistry

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

1264-1269

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

Libby, P.R.

Arch. Biochem. Biophys.

203

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

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

Eur. J. Biochem.

148

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

Wittich, R.M.; Walter, R.D.

Biochem. J.

260

265-269

487260

2320051

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

1990

Wittich, R.M.; Walter, R.D.

Mol. Biochem. Parasitol.

38

13-18

487261

4841346

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

1974

Seiler, N.; Al-Therib, J.

Biochim. Biophys. Acta

354

206-212

487854

16665629

Evidence for transglutaminase activity in plant tissue

1987

Icekson, I.; Apelbaum, A.

Plant Physiol.

84

972-974

489861

6798961

Specificity of mammalian spermidine synthase and spermine synthase

1981

Pegg, A.E.; Shuttleworth, K.; Hibasami, H.

Biochem. J.

197

315-320

489867

6621389

Inhibition of aminopropyltransferases

1983

Pegg, A.E.

Methods Enzymol.

94

294-297

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

1965

Strecker, H.J.

J. Biol. Chem.

240

1225-1230

637121

7287630

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

1981

Yasuda, M.; Tanizawa, K.; Misono, H.; Toyama, S.; Soda, K.

J. Bacteriol.

148

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.

Biochem. J.

219

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

2480-2486

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.

Arch. Biochem. Biophys.

216

213-222

639710

10945218

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

2000

Graser, G.; Hartmann T.

Planta

211

239-245

639718

11731804

The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor

2002

Korolev, S.; Ikeguchi, Y.; Skarina T.; Beasley, S.; Arrowsmith, C.; Edwards, A.; Joachimiak, A.; Pegg, A.E.; Savchenko, A.

Nat. Struct. Biol.

9

27-31

639950

14154456

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

1964

Kim, K.H.

J. Biol. Chem.

239

783-786

639951

-

Diamine-alpha-ketoglutarate aminotransferase (Escherichia coli)

1971

Kim, K.H.; Tchen, T.T.

Methods Enzymol.

17B

812-815

639953

2492500

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

1989

Madduri, K.; Stuttard, C.; Vining, L.C.

J. Bacteriol.

171

299-302

640045

13938132

gamma, delta-Dioxovalerate aminotransferase activity in Rhodopseudomonas spheroides

1963

Neuberger, A.; Turner, J.M.

Biochim. Biophys. Acta

67

342-345

641409

4356198

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

1973

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

Int. J. Vitam. Nutr. Res.

43

318-323

643354

4354232

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

1973

Lazarus, L.H.; Itin, A.

Arch. Biochem. Biophys.

156

154-160

649722

11736657

Identification of essential active-site residues in ornithine decarboxylase of Nicotiana glutinosa decarboxylating both L-ornithine and L-lysine

2001

Lee, Y.S.; Cho, Y.D.

Biochem. J.

360

657-665

650473

12974388

The activator-binding site of Onchocerca volvulus S-adenosylmethionine decarboxylase, a potential drug target

2003

Ndjonka, D.; Zou, Y.; Bi, X.; Woster, P.; Walter, R.D.; Luersen, K.

Biol. Chem.

384

1195-1201

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