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Ligand agmatine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

polyamine pathway

KEGG

Arginine and proline metabolism

MetaCyc

arginine dependent acid resistance, hordatine biosynthesis, L-arginine degradation III (arginine decarboxylase/agmatinase pathway), L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway), putrescine biosynthesis I, putrescine biosynthesis II, spermidine biosynthesis III more

Show all BRENDA pathways known for agmatine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Natural Substrate (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.64

4-coumaroyl-CoA + agmatine = CoA + 4-coumaroylagmatine

758017, 487360

-

2.3.1.64

feruloyl-CoA + agmatine = CoA + feruloyl agmatine

706386

-

2.3.1.64

feruloyl-CoA + agmatine = CoA + feruloylagmatine

758017

-

2.3.1.64

p-coumaroyl-CoA + agmatine = CoA + p-coumaroylagmatine

706386

-

2.3.1.64

4 entries

2.4.2.31

NAD+ + agmatine = nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine

735686

4xzk, 3D-view

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + agmatine = 5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine

719718

-

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + agmatine = 5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine

719832, 719710

-

2.5.1.104

2 entries

3.5.3.11

agmatine + H2O = putrescine + urea

246676, 246680, 246683, 710833, 246682, 712119, 754341, 246674, 246677, 246675, 727122, 734651, 753719

7lol, 3D-view

3.5.3.12

agmatine + H2O = N-carbamoylputrescine + NH3

209397, 209396, 209401, 209402, 209395, 209398, 209404, 209399, 209403, 209400, 735102, 209405, 733510, 734228, 734787, 733200, 692430, 752712, 747848, 752778

-

6.3.4.22

ATP + agmatine + [tRNAIle2]-cytidine34 = [tRNAIle2]-2-agmatinylcytidine34 + ?

705848

6agg, 3D-view

6.3.4.22

ATP + agmatine + [tRNAIle2]-cytidine34 = [tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate

720531

6agg, 3D-view

6.3.4.22

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.3.20

1,4-diguanidinobutane + H2O = agmatine + urea

209443, 209444

-

4.1.1.19

L-arginine = agmatine + CO2

-

1mt1, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

-

1n13, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

-

2qqc, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

-

2qqd, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

-

3n2o, 3D-view

4.1.1.19

5 entries

Substrate in Enzyme-catalyzed Reactions (34 results)

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Show Substrate (34 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.13

agmatine + O2 + H2O = ?

671973

-

1.4.3.21

agmatine + H2O + O2 = ?

743003

-

1.4.3.22

agmatine + H2O + O2 = ?

655478, 656323

-

1.4.3.22

agmatine + H2O + O2 = ? + NH3 + H2O2

688193

-

1.4.3.22

agmatine = ?

391940, 391941, 391959, 391945, 391947

-

1.4.3.22

3 entries

2.3.1.138

feruloyl-CoA + agmatine = CoA + N-feruloylagmatine

757363

-

2.3.1.64

4-coumaroyl-CoA + agmatine = CoA + 4-coumaroylagmatine

487360, 487363, 758017, 487362, 487361

-

2.3.1.64

caffeoyl-CoA + agmatine = CoA + caffeoylagmatine

487361, 487362, 487363

-

2.3.1.64

cinnamoyl-CoA + agmatine = CoA + cinnamoyl agmatine

487362

-

2.3.1.64

feruloyl-CoA + agmatine = CoA + feruloyl agmatine

487361, 487362, 487363, 706386

-

2.3.1.64

feruloyl-CoA + agmatine = CoA + feruloylagmatine

758017

-

2.3.1.64

p-coumaroyl-CoA + agmatine = CoA + p-coumaroylagmatine

706386

-

2.3.1.64

sinapoyl-CoA + agmatine = CoA + sinapoyl agmatine

487362

-

2.4.2.31

agmatine + NAD+ = nicotinamide + ?

638115, 638094, 638100, 638101, 638102, 722180, 638124, 638117

4xzk, 3D-view

2.4.2.31

NAD+ + agmatine = nicotinamide + Nomega-(ADP-D-ribosyl)-agmatine

759729, 735686

4xzk, 3D-view

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + agmatine = 5'-S-methyl-5'-thioadenosine + N1-aminopropylagamatine

719718

-

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + agmatine = 5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine

719718, 719832, 719710

-

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + agmatine = S-methyl-5'-thioadenosine + N1-aminopropylagmatine

720250

-

2.3.1.64

7 entries

2.4.2.31

2 entries

2.5.1.104

3 entries

2.6.1.82

agmatine + 2-oxoglutarate = ?

661399

-

2.7.3.10

ATP + agmatine = ADP + N4-phosphoagmatine

642370

-

3.4.22.70

agmatine + YALPETGK = (NH2)2-CN-(CH2)4-NH-(CO)-TEPLAY + ?

717831

-

3.5.3.1

agmatine + H2O = 1,4-diaminobutane + urea

668975, 668556, 669279

-

3.5.3.11

agmatine + H2O = putrescine + urea

246676, 246680, 246681, 246683, 649495, 710833, 246682, 712119, 754341, 246674, 246677, 664200, 246675, 695474, 726980, 727122, 734651, 753719, 686646

7lol, 3D-view

3.5.3.12

agmatine + ADP + phosphate = ATP + putrescine + NH3 + CO2

209403

-

3.5.3.12

agmatine + H2O = N-carbamoylputrescine + NH3

209397, 209396, 209401, 209402, 209395, 209398, 209404, 670510, 209399, 209403, 209400, 735102, 718884, 657259, 209405, 733510, 734228, 734787, 687349, 747848, 692430, 713057, 733200, 752712, 752778, 711375, 655571, 669131, 669081, 653166, 674316, 695768

-

3.5.3.12

agmatine + H2O = NH3 + N-carbamoylputrescine

700535, 692430

-

3.5.3.12

agmatine + H2O = putrescine + ?

685687

-

3.5.3.12

agmatine + ornithine + H2O + phosphate = putrescine + citrulline + NH3 + phosphate

209399, 209403

-

3.5.3.12

5 entries

3.5.3.15

agmatine + H2O = ? + NH3

733075

-

3.5.3.16

agmatine + H2O = ?

209433

-

3.5.3.20

agmatine + H2O = putrescine + urea

209443, 209444

-

3.5.3.24

agmatine + H2O = putrescine + urea

719718

-

6.3.4.22

ATP + agmatine + [tRNAIle2]-cytidine34 = [tRNAIle2]-2-agmatinylcytidine34 + ?

705848

6agg, 3D-view

6.3.4.22

ATP + agmatine + [tRNAIle2]-cytidine34 = [tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate

720531

6agg, 3D-view

6.3.4.22

2 entries

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.40

acetyl agmatine + H2O = acetic acid + agmatine

172038

-

3.5.1.40

benzoyl agmatine + H2O = benzoic acid + agmatine

172038

-

3.5.1.40

bleomycin B2 + H2O = bleomycinic acid + agmatine

172038, 172037

-

3.5.1.40

propionyl agmatine + H2O = propionic acid + agmatine

172038

-

3.5.1.40

4 entries

3.5.3.20

1,4-diguanidinobutane + H2O = agmatine + urea

209443, 209444

-

4.1.1.17

Arg = 1-Amino-4-guanidinobutane

-

-

4.1.1.19

L-arginine = agmatine + CO2

4072, , 4019, 4084, 4085, 4086, 4089, 4090, 4092, 4096, 4098, 4097, 4100, 4099, 4076, 4091, 4094, 4074, 4080, 4081, 4093, 4082, 4083, 4087, 4077, 4088, 4078, 4095, 4073, 4079, 4101

1mt1, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

4072, , 4019, 4084, 4085, 4086, 4089, 4090, 4092, 4096, 4098, 4097, 4100, 4099, 4076, 4091, 4094, 4074, 4080, 4081, 4093, 4082, 4083, 4087, 4077, 4088, 4078, 4095, 4073, 4079, 4101

1n13, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

4072, , 4019, 4084, 4085, 4086, 4089, 4090, 4092, 4096, 4098, 4097, 4100, 4099, 4076, 4091, 4094, 4074, 4080, 4081, 4093, 4082, 4083, 4087, 4077, 4088, 4078, 4095, 4073, 4079, 4101

2qqc, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

4072, , 4019, 4084, 4085, 4086, 4089, 4090, 4092, 4096, 4098, 4097, 4100, 4099, 4076, 4091, 4094, 4074, 4080, 4081, 4093, 4082, 4083, 4087, 4077, 4088, 4078, 4095, 4073, 4079, 4101

2qqd, 3D-view

4.1.1.19

L-arginine = agmatine + CO2

4072, , 4019, 4084, 4085, 4086, 4089, 4090, 4092, 4096, 4098, 4097, 4100, 4099, 4076, 4091, 4094, 4074, 4080, 4081, 4093, 4082, 4083, 4087, 4077, 4088, 4078, 4095, 4073, 4079, 4101

3n2o, 3D-view

4.1.1.19

5 entries

4.1.1.B12

L-arginine = agmatine + CO2

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.5.3.12

-

700535

-

Inhibitor in Enzyme-catalyzed Reactions (44 results)

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Show Inhibitors (44 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.39

at lower concentration than the Ki value agmatine leads to time-, concentration-, NADPH- and calmodulin-dependent inhibition of the neuronal enzyme in presence of calmodulin; causes an increase in NADPH oxidase activity of the enzyme

440233

-

1.4.3.10

-

395447

-

1.5.3.14

-

392421

-

1.5.3.14

competitive inhibition of spermidine oxidation

705043

-

1.5.3.14

2 entries

1.5.3.16

-

676604

-

2.1.3.3

13 mM, 50% inhibition

485916

-

2.3.1.109

-

486122

-

2.3.1.64

the presence of this substrate inhibits the enzyme reaction with putrescine

706386

-

2.5.1.16

89% inhibition at 0.1 mM and 61% inhibition at 1 mM

639710

-

2.7.3.1

-

642364

-

2.7.3.3

10 mM, 79.3% inhibition

662528

-

2.7.3.3

5fold higher concentration than L-Arg, 20% inhibition

642482

-

2.7.3.3

61% enzyme inhibition at 2 mM

738179

-

2.7.3.3

65% inhibition at 2 mM

738179

-

2.7.3.3

4 entries

3.4.21.74

-

29684

-

3.4.21.83

reversible

669308

-

3.4.24.20

caseinolytic activity

31047

-

3.5.3.1

-

172127, 654612

-

3.5.3.1

poor arginase 1 inhibitor

755503

-

3.5.3.12

above 8 mM slight substrate inhibition

209401

-

3.5.3.12

AgDS-deficient strain is unable to grow in the presence of 20 mM agmatine, suggesting that AgDS converts a growth-inhibitory substance into products that can enhance acid tolerance

669131

-

3.5.3.1

2 entries

3.5.3.12

2 entries

3.5.3.20

28% inhibition at concentration of 5.0 mM

209444

-

3.5.3.6

-

209453, 209460

-

3.5.3.6

10 mM, 8% loss of activity. 200 mM, 28% loss of activity

754217

-

3.5.3.6

very weak, mixed-type inhibitor

711372

-

3.5.3.6

3 entries

3.5.3.7

-

209481

-

4.1.1.17

1 mM, 77% inhibition

651824

-

4.1.1.17

non-competitive

4037

-

4.1.1.19

-

4080, 4082, 4083, 4085, 4086, 4099, 4100, 4101, 654689

1mt1, 3D-view

4.1.1.19

-

4080, 4082, 4083, 4085, 4086, 4099, 4100, 4101, 654689

1n13, 3D-view

4.1.1.19

-

4080, 4082, 4083, 4085, 4086, 4099, 4100, 4101, 654689

2qqc, 3D-view

4.1.1.19

-

4080, 4082, 4083, 4085, 4086, 4099, 4100, 4101, 654689

2qqd, 3D-view

4.1.1.19

-

4080, 4082, 4083, 4085, 4086, 4099, 4100, 4101, 654689

3n2o, 3D-view

4.1.1.19

1.4 mM, 50% inhibition

656053

1mt1, 3D-view

4.1.1.19

1.4 mM, 50% inhibition

656053

1n13, 3D-view

4.1.1.19

1.4 mM, 50% inhibition

656053

2qqc, 3D-view

4.1.1.19

1.4 mM, 50% inhibition

656053

2qqd, 3D-view

4.1.1.19

1.4 mM, 50% inhibition

656053

3n2o, 3D-view

4.1.1.19

10 mM, 57% inhibition

4078

1mt1, 3D-view

4.1.1.19

10 mM, 57% inhibition

4078

1n13, 3D-view

4.1.1.19

10 mM, 57% inhibition

4078

2qqc, 3D-view

4.1.1.19

10 mM, 57% inhibition

4078

2qqd, 3D-view

4.1.1.19

10 mM, 57% inhibition

4078

3n2o, 3D-view

4.1.1.17

2 entries

4.1.1.19

15 entries

4.1.1.50

-

4691

-

3D Structure of Enzyme-Ligand-Complex (PDB) (39 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (39 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.5.1.11

3iqd, 3D-view

2.4.2.31

4xzk, 3D-view

2.5.1.44

4xqe, 3D-view

2.5.1.44

4xqg, 3D-view

2.5.1.44

4xr4, 3D-view

2.5.1.44

4xrg, 3D-view

2.5.1.44

6s3x, 3D-view

2.5.1.44

6s49, 3D-view

2.5.1.44

4xqe, 3D-view

2.5.1.44

4xqg, 3D-view

2.5.1.44

4xr4, 3D-view

2.5.1.44

4xrg, 3D-view

2.5.1.44

6s3x, 3D-view

2.5.1.44

6s49, 3D-view

2.5.1.44

4xqe, 3D-view

2.5.1.44

4xqg, 3D-view

2.5.1.44

4xr4, 3D-view

2.5.1.44

4xrg, 3D-view

2.5.1.44

6s3x, 3D-view

2.5.1.44

6s49, 3D-view

2.5.1.44

18 entries

3.4.21.4

1aq7, 3D-view

3.4.22.38

4yv8, 3D-view

3.5.3.11

7lol, 3D-view

4.1.1.19

1mt1, 3D-view

4.1.1.19

1n13, 3D-view

4.1.1.19

2qqc, 3D-view

4.1.1.19

2qqd, 3D-view

4.1.1.19

3n2o, 3D-view

4.1.1.19

1mt1, 3D-view

4.1.1.19

1n13, 3D-view

4.1.1.19

2qqc, 3D-view

4.1.1.19

2qqd, 3D-view

4.1.1.19

3n2o, 3D-view

4.1.1.19

1mt1, 3D-view

4.1.1.19

1n13, 3D-view

4.1.1.19

2qqc, 3D-view

4.1.1.19

2qqd, 3D-view

4.1.1.19

3n2o, 3D-view

4.1.1.19

15 entries

6.3.4.22

6agg, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (25 results)

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Show Turnover Number (25 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.22

6.5

-

pH 8.5, 25°C

688193

1.4.3.22

45.9

-

pH 7.2, 25°C

655478, 688193

2.5.1.104

0.1

-

pH 7.4, 70°C

719710

2.5.1.104

0.28

-

pH 9.0, 70°C

719718

2.5.1.104

0.37

-

pH 9.0, 37°C

719832, 720250

3.5.3.11

0.0075

-

pH 7.5, 70°C, mutant enzyme C71S

726980

3.5.3.11

0.0095

-

pH 7.5, 70°C, mutant enzyme C151S

726980

3.5.3.11

0.023

-

pH 7.5, 70°C, mutant enzyme C136A

726980

3.5.3.11

0.032

-

pH 7.5, 70°C, wild-type enzyme

726980

3.5.3.11

0.041

-

pH 7.5, 70°C, mutant enzyme C229A

726980

3.5.3.11

0.7

-

mutant enzyme H435A, pH 9.0, 37°C

754341

3.5.3.11

0.9

-

mutant enzyme H206A, pH 9.0, 37°C

754341

3.5.3.11

1

-

mutant enzyme H394A, pH 9.0, 37°C

754341

3.5.3.11

1

-

wild-type enzyme, pH 9.0, 37°C

754341

3.5.3.11

1.1

-

mutant enzyme H65A, pH 9.0, 37°C

754341

3.5.3.11

1.7

-

mutant enzyme H127A, pH 9.0, 37°C

754341

3.5.3.11

3

-

-

686646

3.5.3.12

0.0047

-

mutant D198A, pH 8.0, 37°C

711375

3.5.3.12

0.00533

-

pH 7.0, 37°C

752778

3.5.3.12

0.082

-

wild-type, pH 8.0, 37°C

711375

3.5.3.12

0.517

-

pH 7.5, 25°C

752712

3.5.3.12

8

-

-

653166

3.5.3.12

34.28

-

at 25°C and pH 7.5

734228

1.4.3.22

2 entries

2.5.1.104

3 entries

3.5.3.11

12 entries

3.5.3.12

6 entries

3.5.3.24

0.00186

-

pH 7.5, 70°C

719718

6.3.4.22

0.006

-

pH 8.8, 70°C

720531

K_M Value (56 results)

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Show KM Value (56 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.22

0.017

-

pH 8.5, 25°C

688193

1.4.3.22

0.49

-

pH 7.2, 25°C

688193

1.4.3.22

0.5

-

-

391959

2.3.1.138

0.1755

-

cosubstrate 4-coumaroyl-CoA, pH 7.5, 30°C

757363

2.3.1.138

0.322

-

cosubstrate feruloyl-CoA, pH 7.5, 30°C

757363

2.3.1.64

0.0052

-

isoenzyme 1

487363

2.3.1.64

0.0052

-

isoenzyme 3

487363

2.3.1.64

0.0065

-

isoenzyme 2

487363

2.3.1.64

0.0081

-

recombinant enzyme

487363

2.3.1.64

0.0095

-

-

487362

2.3.1.64

0.012

-

-

487361

2.4.2.31

0.26

-

-

638101

2.4.2.31

1

-

-

638100

2.4.2.31

2

-

NAD:arginine ADP-ribosyltransferase A

638102

2.4.2.31

9.4

-

enzyme Yac-1

638124

2.4.2.31

15

-

enzyme Yac-2

638124

2.5.1.104

0.0076

-

pH 7.4, 70°C

719710

2.5.1.104

0.012

-

pH 9.0, 70°C

719718

2.5.1.104

0.77

-

pH 9.0, 37°C

719832, 720250

1.4.3.22

3 entries

2.3.1.138

2 entries

2.3.1.64

6 entries

2.4.2.31

5 entries

2.5.1.104

3 entries

3.4.22.70

1.18

-

at 37°C, pH not specified in the publication, transpeptidation reaction

717831

3.5.3.1

2.5

-

37°C, pH 9.0, mutant N149D

668556

3.5.3.11

0.53

-

50°C, pH 11.3

664200

3.5.3.11

1.1

-

mutant enzyme H127A, pH 9.0, 37°C

754341

3.5.3.11

1.1

-

mutant enzyme H394A, pH 9.0, 37°C

754341

3.5.3.11

1.1

-

wild type

649495

3.5.3.11

1.2

-

-

246681

3.5.3.11

1.2

-

mutant enzyme H206A, pH 9.0, 37°C

754341

3.5.3.11

1.4

-

-

686646

3.5.3.11

1.7

-

mutant enzyme H435A, pH 9.0, 37°C

754341

3.5.3.11

2.4

-

pH 7.5, 70°C, wild-type enzyme

726980

3.5.3.11

2.5

-

wild-type enzyme, pH 9.0, 37°C

754341

3.5.3.11

3.6

-

mutant enzyme H65A, pH 9.0, 37°C

754341

3.5.3.11

5.3

-

-

246682

3.5.3.11

5.8

-

pH 7.5, 70°C, mutant enzyme C229A

726980

3.5.3.11

6.2

-

pH 7.5, 70°C, mutant enzyme C151S

726980

3.5.3.11

6.3

-

mutant E274A

649495

3.5.3.11

6.4

-

-

246677

3.5.3.11

9.2

-

pH 7.5, 70°C, mutant enzyme C136A

726980

3.5.3.11

11

-

pH 7.5, 70°C, mutant enzyme C71S

726980

3.5.3.12

0.012

-

-

670510

3.5.3.12

0.016

-

pH 7.0, 30°C

657259

3.5.3.12

0.033

-

wild-type, pH 8.0, 37°C

711375

3.5.3.12

0.07

-

pH 7.0, 37°C

752778

3.5.3.12

0.17

-

mutant D198A, pH 8.0, 37°C

711375

3.5.3.12

0.19

-

-

209398, 209404

3.5.3.12

0.33

-

pH 7.5, 25°C

752712

3.5.3.12

0.6

-

-

653166

3.5.3.12

0.65

-

at 25°C and pH 7.5

734228

3.5.3.12

0.76

-

-

209397, 209398

3.5.3.12

0.8

-

-

209401

3.5.3.12

2.5

-

-

209404

3.5.3.12

6.67

-

-

685687

3.5.3.12

15

-

-

209402, 209404

3.5.3.11

18 entries

3.5.3.12

14 entries

3.5.3.20

3

-

-

209444

3.5.3.24

0.486

-

pH 7.5, 70°C

719718

6.3.4.22

0.00087

-

pH 8.8, 70°C

720531

K_i Value (9 results)

top print hide

Show KI Value (9 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.39

0.66

-

at lower concentration than the Ki value agmatine leads to time-, concentration-, NADPH- and calmodulin-dependent inhibition of the neuronal enzyme in presence of calmodulin

440233

1.4.3.10

0.036

-

-

395447

1.5.3.14

0.003

-

-

392421

1.5.3.14

0.003

-

pH 6.5, 25°C

705043

1.5.3.14

2 entries

1.5.3.16

0.147

-

pH 8.0, substrate: spermine

676604

2.3.1.109

3.4

-

-

486122

3.4.21.83

0.188

-

pH 8.0, 37°C, native enzyme

669308

3.4.21.83

0.207

-

pH 8.0, 37°C, recombinant enzyme

669308

3.4.21.83

2 entries

4.1.1.19

2.77

-

pH 7.5, 37°C

654689

References & Links

Literature References (156)

top print hide

Show Reference (156 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4019

6353148

Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli

1983

Morris, D.R.; Boeker, E.A.

Methods Enzymol.

94

125-134

4037

2241895

Characterization of a high affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans

1990

Schaeffer, J.M.; Donatelli, M.R.

Biochem. J.

270

599-604

4072

16664442

Activities of arginine and ornithine decarboxylases in various plant species

1985

Birecka, H.; Bitonti, A.J.; McCann, P.P.

Plant Physiol.

79

515-519

4073

16663805

Partial purification and characterization of arginine decarboxylase from avocado fruit, a thermostable enzyme

1984

Winer, L.; Vinkler, C.; Apelbaum, A.

Plant Physiol.

76

233-237

4074

-

Arginine decarboxylase (oat seedlings)

1983

Smith, T.A.

Methods Enzymol.

94

176-180

4076

16662531

Ornithine decarboxylase and arginine decarboxylase activities in meristematic tissue of tomato and potato plants

1982

Cohen, E.; Heimer, Y.M.; Mizrahi, Y.

Plant Physiol.

70

544-546

4077

16662312

Arginine and ornithine decarboxylase, the polyamine biosynthetic enzymes of mung bean seedlings

1982

Altman, A.; Friedman, R.; Levin, N.

Plant Physiol.

69

876-879

4078

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Purification and partial characterization of arginine decarboxylase from rice embryos (Oryza sativa L.)

1982

Choudhuri, M.M.; Ghosh, B.

Agric. Biol. Chem.

46

739-743

4079

-

Location of several enzymes of L-arginine catabolism in Evernia prunastri thallus

1981

Legaz, E.; Vicente, C.

Z. Naturforsch. C

36

692-693

4080

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Arginine decarboxylase of oat seedlings

1979

Smith, T.A.

Phytochemistry

18

1447-1452

4081

428658

Determination and purification of arginine decarboxylase from oat seedlings

1979

Smith, T.A.; Ng, W.Y.

Biochem. Soc. Trans.

7

391-393

4082

1382

Arginine decarboxylase from a Pseudomonas species

1976

Rosenfeld, H.J.; Roberts, J.

J. Bacteriol.

125

601-607

4083

1252

Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties

1975

Ramakrishna, S.; Adiga, P.R.

Eur. J. Biochem.

59

377-386

4084

4571774

Biosynthetic arginine decarboxylase from E. coli: Biosynthetic arginine decarboxylase from Escherichia coli

1973

Wu, W.H.; Morris, D.R.

J. Biol. Chem.

248

1696-1699

4085

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Arginine decarboxylase (Escherichia coli B)

1971

Boeker, E.A.; Snell, E.E.

Methods Enzymol.

17B

657-662

4086

4870599

Arginine decarboxylase from Escherichia coli: Arginine decarboxylase from escherichia coli. I. Purification and specificity for substrates and coenzyme

1968

Blethen, S.L.; Boeker, E.A.; Snell, E.E.

J. Biol. Chem.

243

1671-1677

4087

3295879

Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells

1987

Kierszenbaum, F.; Wirth, J.J.; McCann, P.P.; Sjoerdsma, A.

Proc. Natl. Acad. Sci. USA

84

4278-4282

4088

17746056

Arginine decarboxylase and polyamines required for embryogenesis in the wild carrot

1984

Feirer, R.P.; Mignon, G.; Litvay, J.D.

Science

223

1433-1435

4089

23144

Arginine decarboxylase from Escherichia coli B: mechanism of dissociation from the decamer to the dimer

1978

Boecker, E.A.

Biochemistry

17

258-263

4090

15561

Kinetics of the decamer - dimer dissociation of arginine decarboxylase

1977

Boeker, A.B.

Biochem. Biophys. Res. Commun.

75

179-185

4091

-

Etude de l'activite de l'arginine decarboxylase dans les jeunes plantes de Glycine max privees de leurs cotyledons

1975

Le Rudulier, D.; Goas, G.

Phytochemistry

14

1723-1725

4092

4942324

Arginine decarboxylase from Escherichia coli

1971

Boecker, E.A.; Fischer, E.H.; Snell, E.

J. Biol. Chem.

246

6776-6781

4093

16652937

Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme

1992

Malmberg, R.L.; Smith, K.E.; Bell, E.; Cellino, M.L.

Plant Physiol.

100

146-152

4094

9399439

Purification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls

1997

Nam, K.H.; Lee, S.H.; Lee, J.

Plant Cell Physiol.

38

1150-1155

4095

-

Purification and synthesis under anaerobic conditions of rice arginine decarboxylase

1994

Reggiani, R.

Plant Cell Physiol.

35

1245-1249

4096

1646785

Cyclic AMP inhibits and putrescine represses expression of the speA gene encoding biosynthetic arginine decarboxylase

1991

Moore, R.C.; Boyle, S.M.

J. Bacteriol.

173

3615-3621

4097

7677342

Agmatine is synthesized by a mitochondrial arginine decarboxylase in rat brain

1995

Li, G.; Regunathan, S.; Reis, D.J.

Ann. N. Y. Acad. Sci.

763

325-329

4098

15299455

Crystallization of biosynthetic arginine decarboxylase from Escherichia coli

1994

Rodriguez, B.R.; Carroll, D.W.; Mitchell, D.; Momany, C.; Hackert, M.L.

Acta Crystallogr. Sect. D

50

175-177

4099

2667997

Modulation of arginine decarboxylase activity from Mycobacterium smegmatis

1989

Balasundaram, D.; Tyagi, A.K.

Eur. J. Biochem.

183

339-345

4100

7543626

Partial cloning and characterization of an arginine decarboxylase in the kidney

1995

Morrissey, J.; McCracken, R.; Ishidoya, S.; Klahr, S.

Kidney Int.

47

1458-1461

4101

-

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

4691

1764068

Purification of S-adenosylmethionine decarboxylase from soybean

1991

Yang, Y.G.; Cho, Y.D.

Biochem. Biophys. Res. Commun.

181

1181-1186

29684

1011992

Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom

1976

Nolan, C.; Hall, L.S.; Barlow, G.H.

Methods Enzymol.

45

205-213

31047

8749321

Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa

1995

Nonaka, T.; Ishikawa, H.; Tsumuraya, Y.; Hashimoto, Y.; Dohmae, N.; Takio, K.

J. Biochem.

118

1014-1020

172037

50318

Characterizations of acylagmatine amidohydrolase and carboxypeptidase from Fusarium anguioides

1975

Takahashi, Y.; Shirai, T.; Ishii, S.

J. Biochem.

77

823-830

172038

4131159

Preparation of bleomycinic acid: Hydrolysis of bleomycin B2 by a Fusarium acylagmatine amidohydrolase

1973

Umezawa, H.; Takahashi, Y.; Fujii, A.; Saino, T.; Shirai, T.; Takita, T.

J. Antibiot.

26

117-119

172127

2029528

Characterization of arginase from the extreme thermophile Bacillus caldovelox

1991

Patchett, M.L.; Daniel, R.M.; Morgan, H.W.

Biochim. Biophys. Acta

1077

291-298

209395

-

Biogenese de la N-carbamylputrescine et de la putrescine dans les plantules de Glycine max (L.) Merr

1980

Le Rudulier, D.; Goas, G.

Physiol. Veg.

18

609-616

209396

-

Agmatine iminohydrolase in maize

1969

Smith, T.A.

Phytochemistry

8

2111-2117

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

209399

6895223

Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)

1981

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

J. Biol. Chem.

256

9532-9541

209400

-

Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis

1982

Simon, J.P.; Stalon, V.

J. Bacteriol.

11

676-681

209401

-

Regulation of agmatine iminohydrolase of Evernia prunastri by L-arginine metabolites

1983

Legaz, M.E.; Iglesias, A.; Vicente, C.

Z. Pflanzenphysiol.

110

53-59

209402

-

Agmatine deiminase in rice seedlings

1985

Chaudhuri, M.M.; Ghosh, B.

Phytochemistry

24

2433-2435

209403

-

Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis

1986

Prasad, G.L.; Adiga, P.R.

J. Biosci.

10

373-391

209404

1989611

Purification of monomeric agmatine iminohydrolase from soybean

1991

Park, K.H.; Cho, Y.D.

Biochem. Biophys. Res. Commun.

174

32-36

209405

-

Differential enzymatic measurement of agmatine, putrescine, and diguanidinobutane

1996

Shoeb, S.M.; Shimizu, E.; Yorifuji, T.

Biosci. Biotechnol. Biochem.

60

69-72

209433

7353662

A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42

1980

Nakajima, M.; Shirokane, Y.; Mizusawa, K.

FEBS Lett.

110

43-46

209443

-

Degradation of alpha,omega-diguanidinoalkanoates and a novel enzyme, diguanidinobutane amidohydrolase in Pseudomonas putida

1989

Yorifuji, T.; Kaneoke, M.; Shimizu, E.; Shiota, K.; Matsuo, R.

Agric. Biol. Chem.

53

3003-3009

209444

-

Diguanidinobutanase of Pseudomonas putida and enzymatic preparation of agmatine from 1,4-diguanidinobutanate

1995

Shoeb, S.M.; Kaneoke, M.; Shimizu, E.; Yorifuji, T.

Appl. Microbiol. Biotechnol.

44

94-99

209453

681336

Arginine deiminase from Mycoplasma arthritidis. Structure-activity relationships among substrates and competitive inhibitors

1978

Smith, D.W.; Ganaway, R.L.; Fahrney, D.E.

J. Biol. Chem.

253

6016-6020

209460

9468500

Cloning and expression of a prokaryotic enzyme, arginine deiminase, from primitive eukaryote Giardia intestinalis

1998

Knodler, L.A.; Sekyere, E.O.; Stewart, T.S.; Schofield, P.J.; Edwards, M.R.

J. Biol. Chem.

273

4470-4477

209481

27286206

Guanidinobutyrase for L-arginine degradation in Brevibacterium helvolum

1992

Yorifuji, T.; Shimizu, E.; Hirata, H.; Imada, K.; Katsumi, T.; Sawamura, S.

Biosci. Biotechnol. Biochem.

56

773-777

246674

35512

Enzymes of agmatine degradation and the control of their synthesis in Klebsiella aerogenes

1979

Friedrich, B.; Magasanik, B.

J. Bacteriol.

137

1127-1133

246675

-

Metabolism of agmatine in fruit-bodies of the fungus Panus tigrinus (bull. ex. fr.) sing.

1971

Boldt, A.; Miersch, J.; Reinbothe, H.

Phytochemistry

10

731-738

246676

10527864

Evidence that histidine-163 is critical for catalytic activity, but not for substrate binding to Escherichia coli agmatinase

1999

Carvajal, N.; Olate, J.; Salas, M.; Lopez, V.; Cerpa, J.; Herrera, P.; Uribe, E.

Biochem. Biophys. Res. Commun.

264

196-200

246677

-

Purification and properties of agmatine amidinohydrolase of Evernia prunastri

1982

Vicente, C.; Legaz, M.E.

Physiol. Plant.

55

335-339

246680

3897201

Metabolic pathway for the utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12

1985

Shaibe, E.; Metzer, E.; Halpern, Y.S.

J. Bacteriol.

163

933-937

246681

3081491

Purification and properties of agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli

1986

Satishchandran, C.; Boyle S.M.

J. Bacteriol.

165

843-848

246682

8858963

Agmatinase activity in rat brain: a metabolic pathway for the degradation of agmatine

1995

Sastre, M.; Regunathan, S.; Galea, E.; Reis, D.J.

J. Neurochem.

67

1761-1765

246683

1310091

Influence of cyclic AMP, agmatine and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli

1992

Szumanski, M.B.W.; Boyle, S.M.

J. Bacteriol.

174

758-764

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

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

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

392421

11342283

Inhibition of pig liver and Zea mays L. polyamine oxidase: a comparative study

2001

Federico, R.; Leone, L.; Botta, M.; Binda, C.; Angelini, R.; Venturini, G.; Ascenzi, P.

J. Enzyme Inhib.

16

147-155

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

440233

11125020

Agmatine enhances the NADPH oxidase activity of neuronal NO synthase and leads to oxidative inactivation of the enzyme

2001

Demady, D.R.; Jianmongkol, S.; Vuletich, J.L.; Bender, A.T.; Osawa, Y.

Mol. Pharmacol.

59

24-29

485916

-

Characterization of ornithine carbamoyltransferase from cultured carrot cells of low embryogenic potential

1983

Baker, S.R.; Yon, R.J.

Phytochemistry

22

2171-2174

486122

7523119

Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine

1994

Tricot, C.; Vander Wauven, C.; Wattiez, R.; Falmagne, P.; Stalon, V.

Eur. J. Biochem.

224

853-861

487360

-

The biosynthesis of coumaroylagmatine in barley seedlings

1981

Bird, C.R.; Smith, T.A.

Phytochemistry

20

2345-2346

487361

-

Agmatine coumaroyltransferase (barley seedlings)

1983

Bird, C.R.; Smith, T.A.

Methods Enzymol.

94

344-347

487362

-

Agmatine coumaroyltransferase from barley seedlings

1983

Bird, C.R.; Smith, T.A.

Phytochemistry

22

2401-2403

487363

12582168

A new class of N-hydroxycinnamoyltransferases. Purification, cloning, and expression of barley agmatine coumaroyltransferase (EC 2.3.1.64)

2003

Burhenne, K.; Kristensen, B.K.; Rasmussen, S.K.

J. Biol. Chem.

278

13919-13927

638094

225315

Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes

1979

Moss, J.; Stanley, S.J.; Oppenheimer, N.J.

J. Biol. Chem.

254

8891-8894

638100

6426504

Activation of an erythrocyte NAD:arginine ADP-ribosyltransferase by lysolecithin and nonionic and zwitterionic detergents

1984

Moss, J.; Osborne, J.C.; Stanley, S.J.

Biochemistry

23

1353-1357

638101

3935159

Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: the soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae

1985

Osborne, J.C.; Stanley, S.J.; Moss, J.

Biochemistry

24

5235-5240

638102

3099839

Amino acid specific ADP-ribosylation: specific NAD: arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes

1986

West, R.E.; Moss, J.

Biochemistry

25

8057-8062

638115

8703012

Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase

1996

Okazaki, I.J.; Kim, H.J.; Moss, J.

J. Biol. Chem.

271

22052-22057

638117

-

Arginine-specific mono(ADP-ribosyl)transferase activity on the surface of human polymorphonuclear neutrophil leukocytes

1996

Donnelly, L.E.; Rendell, N.B.; Murray, S.; Allport, J.R.; Lo, G.; Kefalas, P.; Taylor, G.W.; MacDermot, J.

Biochem. J.

315

635-641

638124

9193645

Molecular cloning and characterization of lymphocyte and muscle ADP-ribosyltransferases

1997

Okazaki, I.J.; Kim, H.J.; Moss, J.

Adv. Exp. Med. Biol.

419

129-136

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

642364

-

Purification and properties of guanidinoacetate kinase from a polychaete, Perineis sp.

1991

Shirokane, Y.; Nakajima, M.; Mizusawa, K.

Agric. Biol. Chem.

55

2235-2242

642370

-

Phosphagens in protozoa - II. Presence of phosphagen kinase in Ochromonas danica

1979

Piccinni, E.; Coppellotti, O.

Comp. Biochem. Physiol. B

62

287-289

642482

10625703

Trypanosoma cruzi arginine kinase characterization and cloning. A novel energetic pathway in protozoan parasites

2000

Pereira, C.A.; Alonso, G.D.; Paveto, M.C.; Iribarren, A.; Cabanas, M.L.; Torres, H.N.; Flawia, M.M.

J. Biol. Chem.

275

1495-1501

649495

15369817

Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group

2004

Carvajal, N.; Orellana, M.S.; Salas, M.; Enriquez, P.; Alarcon, R.; Uribe, E.; Lopez, V.

Arch. Biochem. Biophys.

430

185-190

651824

-

Comparison of biochemical and immunological properties between rat and Nicotiana glutinosa ornithine decarboxylase

2001

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

J. Biochem. Mol. Biol.

34

408-414

653166

12634339

Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway

2003

Nakada, Y.; Itoh, Y.

Microbiology

149

707-714

654612

11478904

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The Formation of lysine tyrosylquinone (LTQ) is a self-processing reaction. Expression and characterization of a Drosophila lysyl oxidase

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The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction

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Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea

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Accumulation of hydroxycinnamic acid amides induced by pathogen infection and identification of agmatine coumaroyltransferase in Arabidopsis thaliana

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Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia

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Characterization and inactivation of an agmatine deiminase from Helicobacter pylori

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Discovery of an operon that participates in agmatine metabolism and regulates biofilm formation in Pseudomonas aeruginosa

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Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS

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A new subfamily of agmatinases present in methanogenic Archaea is Fe(II) dependent

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Arginine decarboxylase and agmatinase: an alternative pathway for de novo biosynthesis of polyamines for development of mammalian conceptuses

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Porphyromonas gingivalis peptidylarginine deiminase substrate specificity

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Putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium

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del Rio, B.; Linares, D.M.; Ladero, V.; Redruello, B.; Fernandez, M.; Martin, M.C.; Alvarez, M.A.

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Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases

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Listeria monocytogenes aguA1, but not aguA2, encodes a functional agmatine deiminase: biochemical characterization of its catalytic properties and roles in acid tolerance

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Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst-forming cyanobacterium Anabaena

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Burnat, M.; Flores, E.

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Prevalence of the lmo0036-0043 gene cluster encoding arginine deiminase and agmatine deiminase systems in Listeria monocytogenes

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Expression of the agmatine deiminase pathway in Enterococcus faecalis is activated by the AguR regulator and repressed by CcpA and PTS(Man) systems

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Suarez, C.; Espariz, M.; Blancato, V.S.; Magni, C.

PLoS ONE

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Characterization of Vis Toxin, a novel ADP-ribosyltransferase from Vibrio splendidus

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Ravulapalli, R.; Lugo, M.R.; Pfoh, R.; Visschedyk, D.; Poole, A.; Fieldhouse, R.J.; Pai, E.F.; Merrill, A.R.

Biochemistry

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Molecular and biochemical characterisation of arginine kinases in Haemonchus contortus and Teladorsagia circumcincta

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Copper amine oxidase 8 regulates arginine-dependent nitric oxide production in Arabidopsis thaliana

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The relationship among tyrosine decarboxylase and agmatine deiminase pathways in Enterococcus faecalis

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Structural and functional basis for targeting Campylobacter jejuni agmatine deiminase to overcome antibiotic resistance

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Shek, R.; Dattmore, D.A.; Stives, D.P.; Jackson, A.L.; Chatfield, C.H.; Hicks, K.A.; French, J.B.

Biochemistry

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Role and dynamics of an agmatinase-like protein (AGM-1) in Neurospora crassa

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Purification and characterization of arginine deiminase from Pseudomonas putida Structural insights of the differential affinities of L-arginine analogues

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Insight on the interaction of an agmatinase-like protein with Mn(2+) activator ions

2015

Quinones, M.; Cofre, J.; Benitez, J.; Garcia, D.; Romero, N.; Gonzalez, A.; Carvajal, N.; Garcia, M.; Lopez, V.; Schenk, G.; Uribe, E.

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Homoarginine and inhibition of human arginase activity kinetic characterization and biological relevance

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Tommasi, S.; Elliot, D.J.; Da Boit, M.; Gray, S.R.; Lewis, B.C.; Mangoni, A.A.

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Molecular evidence for biochemical diversification of phenolamide biosynthesis in rice plants

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Jasmonic acid/ethylene signaling coordinates hydroxycinnamic acid amides biosynthesis through ORA59 transcription factor

2018

Li, J.; Zhang, K.; Meng, Y.; Hu, J.; Ding, M.; Bian, J.; Yan, M.; Han, J.; Zhou, M.

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Mono-ADP-ribosylation catalyzed by arginine-specific ADP-ribosyltransferases

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