Information on EC 2.3.1.64 - agmatine N4-coumaroyltransferase

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.00036 - 0.00221

4-coumaroyl-CoA

16 entries

0.00313 - 0.205

agmatine

13 entries

0.00187 - 0.0058

caffeoyl-CoA

11 entries

0.00056 - 0.0033

cinnamoyl-CoA

7 entries

0.00057 - 149

feruloyl-CoA

11 entries

0.05

sinapoyl-CoA

0.00036

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.00061

4-coumaroyl-CoA

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

0.00074

4-coumaroyl-CoA

0.000789

4-coumaroyl-CoA

mutant enzyme W376A of isoform ACT1-1, at pH 7.5 and 25°C

0.00092

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00097

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.001

4-coumaroyl-CoA

isoenzyme 1

0.00106

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00108

4-coumaroyl-CoA

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

0.00112

4-coumaroyl-CoA

at pH 7.5 and 25°C

0.00123

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.0015

4-coumaroyl-CoA

0.0016

4-coumaroyl-CoA

isoenzyme 3

0.0021

4-coumaroyl-CoA

isoenzyme 2

0.0021

4-coumaroyl-CoA

recombinant enzyme

0.00221

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00313

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00387

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.0052

agmatine

isoenzyme 1

0.0052

agmatine

isoenzyme 3

0.0065

agmatine

isoenzyme 2

0.0081

agmatine

recombinant enzyme

0.0095

agmatine

0.012

agmatine

0.0571

agmatine

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

0.131

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.146

agmatine

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

0.162

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.205

agmatine

wild type enzyme, at pH 7.5 and 25°C

0.00187

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00191

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00199

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.0028

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00285

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00291

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.0033

caffeoyl-CoA

0.0043

caffeoyl-CoA

isoenzyme 2

0.0043

caffeoyl-CoA

recombinant enzyme

0.0053

caffeoyl-CoA

isoenzyme 3

0.0058

caffeoyl-CoA

isoenzyme 1

0.00056

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00074

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.00112

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00126

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.00201

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00233

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.0033

cinnamoyl-CoA

0.00057

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.0008

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.00088

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

0.0013

feruloyl-CoA

0.0017

feruloyl-CoA

isoenzyme 3

0.00256

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.0041

feruloyl-CoA

isoenzyme 2

0.0061

feruloyl-CoA

isoenzyme 1

0.0066

feruloyl-CoA

recombinant enzyme

125

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

149

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.013 - 51

4-coumaroyl-CoA

9 entries

1.17 - 54.5

agmatine

7 entries

0.008 - 20.1

caffeoyl-CoA

0.023 - 110

cinnamoyl-CoA

0.01 - 34

feruloyl-CoA

0.013

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

0.068

4-coumaroyl-CoA

mutant enzyme W376A of isoform ACT1-1, at pH 7.5 and 25°C

1.33

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

1.38

4-coumaroyl-CoA

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

3.22

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

4.73

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

9.3

4-coumaroyl-CoA

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

9.43

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

1.17

agmatine

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

3.92

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

6.4

agmatine

wild type enzyme, at pH 7.5 and 25°C

10.9

agmatine

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

12.2

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

19.8

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

54.5

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.008

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

6.28

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

8.79

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

13.1

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

20.1

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.023

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

16.3

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

16.9

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

21.9

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

24.1

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

110

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

0.01

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

8.53

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

16.7

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

18.1

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

22.7

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

13 - 55400

4-coumaroyl-CoA

9 entries

8 - 14100

agmatine

7 entries

4 - 10500

caffeoyl-CoA

10 - 54600

cinnamoyl-CoA

4 - 59600

feruloyl-CoA

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

4-coumaroyl-CoA

mutant enzyme W376A of isoform ACT1-1, at pH 7.5 and 25°C

1460

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

2270

4-coumaroyl-CoA

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

3720

4-coumaroyl-CoA

wild type enzyme, at pH 7.5 and 25°C

4470

4-coumaroyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

7670

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

8590

4-coumaroyl-CoA

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

55400

4-coumaroyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

agmatine

mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

agmatine

wild type enzyme, at pH 7.5 and 25°C

agmatine

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

190

agmatine

mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C

6330

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

14100

agmatine

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

3140

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

3360

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

3510

caffeoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

4510

caffeoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

10500

caffeoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

15100

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

19200

cinnamoyl-CoA

wild type enzyme, at pH 7.5 and 25°C

22000

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

39000

cinnamoyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

54600

cinnamoyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

10700

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

12200

feruloyl-CoA

wild type enzyme, at pH 7.5 and 25°C

13400

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

25900

feruloyl-CoA

wild type enzyme isoform ACT2, at pH 7.5 and 25°C

59600

feruloyl-CoA

wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.00000003

with substrates p-coumaroyl-CoA + agmatine + putrescine 0.0018 nmol coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.000000085

with substrates feruloyl-CoA + putrescine 0.0051 nmol feruloylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.000000933

with substrates p-coumaroyl-CoA + putrescine 0.056 nmol p-coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.00002

with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 1.2 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.00004

with substrates feruloyl-CoA + agmatine 2.4 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.000112

with substrates p-coumaroyl-CoA + agmatine 6.7 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.000123

with substrates p-coumaroyl-CoA + agmatine + putrescine 7.4 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.000187

show all columns Go to pH Optimum Search

with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 11.2 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5

0.393

1.22

1.78

11.34

recombinant enzyme

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.5

8.5

7.5

7.5

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.9 - 8.1

half-maximal activity at pH 6.9 and pH 8.1

7 - 8

approx. half-maximal activity at pH 7.0 and 8.0

487361, 487362

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

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TEMPERATURE RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

20 - 50

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

cultivar Nipponbare

SwissProt

brenda

UniProt

brenda

ecotype Col-0

UniProt

brenda

wild-type and mutants, infection of rosette leaves with the fungus Alternaria brassicicola strain MAFF237450

brenda

brenda

SwissProt

brenda

barley, cv. claret

brenda

cultivar Betzes

SwissProt

brenda

cv. Proctor

brenda

isoenzymes 1-3

SwissProt

brenda

isoform ACT1-1; cultivars Betzes, Fibersnow, and Wasedori-nijo

SwissProt

brenda

isoform ACT2; cultivars Betzes, Fibersnow, and Wasedori-nijo

A9ZPJ7

SwissProt

brenda

686954

Q84QG5

SwissProt

brenda

cultivar Chinese Spring

UniProt

brenda

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

leaf

cut off rosette leaves infected with the fungus Alternaria brassicicola

brenda

brenda

brenda

shoots, not seeds

brenda

maximal activity 3-4 days after germination at 22°C in the dark

brenda

brenda

brenda

show all columns Go to Localization Search

brenda

brenda

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

2 entries

physiological function

the enzyme catalyzes the formation of hydroxycinnamic acid amides which are effective toxic antimicrobial substances known as phytoalexins and play an important role in plant defense response

metabolism

last step in the synthesis of hydroxycinnamic acid amides in plants (anti-pathogenic metabolites), in Arabidopsis thaliana infected with Alternaria brassicicola p-coumaroylagmatine, feruloylagmatine, p-coumaroylputrescine, and feruloylputrescine are identified as anti-fungal agents in vitro and in vivo

metabolism

the enzyme catalyzes the last reaction of the hydroxycinnamic acid amides biosynthesis

758017

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (107 entries)
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PDB

SCOP

CATH

UNIPROT

ORGANISM

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

40000

48000

1 * 48000, SDS-PAGE

70000

SDS-PAGE

40000

40000

40000

gel filtration

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 50000, SDS-PAGE

monomer

1 * 48000, SDS-PAGE

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapor diffusion method, using 0.08 M sodium cacodylate pH 6.5, 0.16 M magnesium acetate, 16% (v/v) polyethylene glycol 8000, 20% (v/v) glycerol

show all columns Go to Protein Variants Search

isoform ACT2, hanging drop vapor diffusion method, using 100 mM MMT buffer pH 6.5, 25% (w/v) polyethylene glycol 1500

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

E372A

the mutant shows strongly reduced activity compared to the wild type enzyme

E374A

the mutant shows strongly reduced activity compared to the wild type enzyme

H152A

the mutation reduces the activity to 0.03% of that of the the wild type

W376A

the mutant shows strongly reduced activity compared to the wild type enzyme

additional information

enzyme expression in Torenia hybrida leads to accumulation of hydroxycinnamic acids, predominantly p-coumaroylagmatine, in transgenic plants, and the hydroxycinnamic acids are isomerized from the trans-form to the cis-form in planta. The transgenic line which accumulates the highest amount of endogenous hydroxycinnamic acids, i.e. total hydroxycinnamic acids at 47.5 mM, is resistant to the necrotrophic fungus, Botrytis cinerea. The transformants are not significantly resistant to three representative herbivores, Frankliniella occidentalis, Aphis gossypii, and Tetranychus ludeni

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

2-mercaptoethanol stabilizes

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-40°C, concentrated preparation at least 1 month, negligible loss of activity

Go to Purification (commentary) Search

0°C, 100 mM Tris, pH 7.5, 1 mM EDTA, 10 mM 2-mercaptoethanol, 50 mM KCl

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

ammonium sulfate, Biogel A, Sepharose 4B-agmatine

Blue Sepharose, t-butyl-Sepharose, Resource Q, Superose 12 HR

frozen leaves are homogenized in 100 mM Tris buffer, pH 7.5, containing 10 mM 2-mercaptoethanol and 5 mM DTT, centrifugation, supernatant applied to Sephadex G-50 column, fluent used for enzyme assays, or recombinant Escherichia coli cells are harvested and resuspended in 100 mM Tris buffer, pH 7.5, containing 1 mM EDTA, 50 mM NaCl, 10% glycerol, lysed with lysozyme, sonicated, centrifuged, supernatant used for enzyme assays and SDS-PAGE

isoform ACT2 is purified by Talon metal affinity resin column chromatography, anion exchange chromatography, and gel filtration

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Talon metal-affinity resin column chromatography and Superdex 200 gel filtration

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

2 entries

expressed in Escherichia coli B834(DE3)pLysS cells

expressed in Escherichia coli BL21(DE3)pLysS cells

expressed in Escherichia coli BL21CodonPlus(DE3)RP cells

3 entries

expression in Escherichia coli

expression in Torenia hybrida

PCR-amplification, expression in Escherichia coli BL21(DE3)

expressed in Escherichia coli BL21CodonPlus(DE3)RP cells

expressed in Escherichia coli BL21CodonPlus(DE3)RP cells

expressed in Escherichia coli BL21CodonPlus(DE3)RP cells

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

enzyme expression is induced by a combination of jasmonic acid and ethylene. ORA59 binds to the enzyme gene promoter

758017

ORA59 directly binds to the enzyme gene promoter via the GCC-boxes and activates the enzyme gene expression. The ET precursor 1-aminocyclopropane-1-carboxylic acid treatment significantly induces the enzyme gene expression

upon infection with Alternaria brassicicola enzyme activity in leaves increases markedly from near zero to almost 20 nmol/mg protein/h within 24 h coinciding with an increase in gene transcripts and in the synthesis products, that accumulate in the area of the lesion, slow decrease beyond 24 h

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

agriculture

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

487360

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

The biosynthesis of coumaroylagmatine in barley seedlings

Phytochemistry

2345-2346

1981

Hordeum vulgare

brenda

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

Agmatine coumaroyltransferase (barley seedlings)

Methods Enzymol.

344-347

1983

Hordeum vulgare

brenda

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

Agmatine coumaroyltransferase from barley seedlings

Phytochemistry

2401-2403

1983

Hordeum vulgare

brenda

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

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

J. Biol. Chem.

278

13919-13927

2003

Hordeum vulgare (A9ZPJ6), Hordeum vulgare

12582168

brenda

686954

Nomura, T.; Ishizuka, A.; Kishida, K.; Islam, A.K.; Endo, T.R.; Iwamura, H.; Ishihara, A.

Chromosome arm location of the genes for the biosynthesis of hordatines in barley

Genes Genet. Syst.

455-464

2007

Hordeum vulgare (A9ZPJ6), Hordeum vulgare, Triticum aestivum (Q84QG5), Triticum aestivum

18270436

brenda

Muroi, A.; Ishihara, A.; Tanaka, C.; Ishizuka, A.; Takabayashi, J.; Miyoshi, H.; Nishioka, T.

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

Planta

230

517-527

2009

Arabidopsis thaliana

19521717

brenda

Muroi, A.; Matsui, K.; Shimoda, T.; Kihara, H.; Ozawa, R.; Ishihara, A.; Nishihara, M.; Arimura, G.

Acquired immunity of transgenic torenia plants overexpressing agmatine coumaroyltransferase to pathogens and herbivore pests

Sci. Rep.

689

2012

Arabidopsis thaliana (Q9FNP9)

23008754

brenda

758017

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

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

Plant J.

444-457

2018

Arabidopsis thaliana (Q9FNP9), Arabidopsis thaliana

29752755

brenda

Yamane, M.; Takenoya, M.; Yajima, S.; Sue, M.

Crystal structure of barley agmatine coumaroyltransferase, an N-acyltransferase from the BAHD superfamily

Acta Crystallogr. F Struct. Biol. Commun.

590-596

2020

Hordeum vulgare (A9ZPJ6)

33263570

brenda

Huang, L.J.; Zhang, J.; Lin, Z.; Yu, P.; Lu, M.; Li, N.

The AP2/ERF transcription factor ORA59 regulates ethylene-induced phytoalexin synthesis through modulation of an acyltransferase gene expression

J. Cell. Physiol.

239

e30935

2024

Arabidopsis thaliana (Q9FNP9)

36538653

brenda