BRENDA - Enzyme Database
show all sequences of 2.3.1.64

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

Muroi, A.; Ishihara, A.; Tanaka, C.; Ishizuka, A.; Takabayashi, J.; Miyoshi, H.; Nishioka, T.; Planta 230, 517-527 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
PCR-amplification, expression in Escherichia coli BL21(DE3)
Arabidopsis thaliana
Inhibitors
Inhibitors
Commentary
Organism
Structure
agmatine
the presence of this substrate inhibits the enzyme reaction with putrescine
Arabidopsis thaliana
enterokinase
the removal of the thioredoxin domain by enterokinase decreases the enzyme activity but does not alter the relative amounts of products
Arabidopsis thaliana
additional information
putrescine or feruloyl-CoA do not inhibit the enzyme reaction with agmantine and p-coumaroyl-CoA
Arabidopsis thaliana
p-Coumaroyl-CoA
the presence of this substrate inhibits the enzyme reaction with feruloyl-CoA
Arabidopsis thaliana
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
SDS-PAGE
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
feruloyl-CoA + agmatine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + feruloyl agmatine
-
-
?
feruloyl-CoA + putrescine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + feruloylputrescine
-
-
?
p-coumaroyl-CoA + agmatine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + p-coumaroylagmatine
-
-
?
p-coumaroyl-CoA + putrescine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + p-coumaroylputrescine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
-
wild-type and mutants, infection of rosette leaves with the fungus Alternaria brassicicola strain MAFF237450
-
Purification (Commentary)
Commentary
Organism
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
Arabidopsis thaliana
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
cut off rosette leaves infected with the fungus Alternaria brassicicola
Arabidopsis thaliana
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00000003
-
with substrates p-coumaroyl-CoA + agmatine + putrescine 0.0018 nmol coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000000085
-
with substrates feruloyl-CoA + putrescine 0.0051 nmol feruloylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000000933
-
with substrates p-coumaroyl-CoA + putrescine 0.056 nmol p-coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.00002
-
with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 1.2 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.00004
-
with substrates feruloyl-CoA + agmatine 2.4 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000112
-
with substrates p-coumaroyl-CoA + agmatine 6.7 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000123
-
with substrates p-coumaroyl-CoA + agmatine + putrescine 7.4 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000187
-
with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 11.2 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
feruloyl-CoA + agmatine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + feruloyl agmatine
-
-
-
?
feruloyl-CoA + putrescine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + feruloylputrescine
-
-
-
?
p-coumaroyl-CoA + agmatine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + p-coumaroylagmatine
-
-
-
?
p-coumaroyl-CoA + putrescine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + p-coumaroylputrescine
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
PCR-amplification, expression in Escherichia coli BL21(DE3)
Arabidopsis thaliana
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
agmatine
the presence of this substrate inhibits the enzyme reaction with putrescine
Arabidopsis thaliana
enterokinase
the removal of the thioredoxin domain by enterokinase decreases the enzyme activity but does not alter the relative amounts of products
Arabidopsis thaliana
additional information
putrescine or feruloyl-CoA do not inhibit the enzyme reaction with agmantine and p-coumaroyl-CoA
Arabidopsis thaliana
p-Coumaroyl-CoA
the presence of this substrate inhibits the enzyme reaction with feruloyl-CoA
Arabidopsis thaliana
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
SDS-PAGE
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
feruloyl-CoA + agmatine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + feruloyl agmatine
-
-
?
feruloyl-CoA + putrescine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + feruloylputrescine
-
-
?
p-coumaroyl-CoA + agmatine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + p-coumaroylagmatine
-
-
?
p-coumaroyl-CoA + putrescine
Arabidopsis thaliana
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
CoA + p-coumaroylputrescine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
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
Arabidopsis thaliana
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
cut off rosette leaves infected with the fungus Alternaria brassicicola
Arabidopsis thaliana
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00000003
-
with substrates p-coumaroyl-CoA + agmatine + putrescine 0.0018 nmol coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000000085
-
with substrates feruloyl-CoA + putrescine 0.0051 nmol feruloylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000000933
-
with substrates p-coumaroyl-CoA + putrescine 0.056 nmol p-coumaroylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.00002
-
with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 1.2 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.00004
-
with substrates feruloyl-CoA + agmatine 2.4 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000112
-
with substrates p-coumaroyl-CoA + agmatine 6.7 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000123
-
with substrates p-coumaroyl-CoA + agmatine + putrescine 7.4 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
0.000187
-
with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 11.2 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
feruloyl-CoA + agmatine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + feruloyl agmatine
-
-
-
?
feruloyl-CoA + putrescine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + feruloylputrescine
-
-
-
?
p-coumaroyl-CoA + agmatine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + p-coumaroylagmatine
-
-
-
?
p-coumaroyl-CoA + putrescine
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
706386
Arabidopsis thaliana
CoA + p-coumaroylputrescine
-
-
-
?
Expression
Organism
Commentary
Expression
Arabidopsis thaliana
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
up
General Information
General Information
Commentary
Organism
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
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
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
Arabidopsis thaliana
Expression (protein specific)
Organism
Commentary
Expression
Arabidopsis thaliana
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
up
Other publictions for EC 2.3.1.64
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721048
Muroi
Acquired immunity of transgeni ...
Arabidopsis thaliana
Sci. Rep.
2
689
2012
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1
1
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1
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9
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-
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1
1
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1
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-
-
-
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-
-
-
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-
-
-
-
-
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-
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-
-
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-
-
-
706386
Muroi
Accumulation of hydroxycinnami ...
Arabidopsis thaliana
Planta
230
517-527
2009
-
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1
-
-
-
4
-
-
-
1
4
-
5
-
-
1
-
-
1
8
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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4
-
-
-
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1
4
-
-
-
1
-
1
8
-
4
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
686954
Nomura
Chromosome arm location of the ...
Hordeum vulgare, Triticum aestivum
Genes Genet. Syst.
82
455-464
2007
-
-
2
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
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-
-
-
-
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-
-
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2
-
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-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
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-
487363
Burhenne
A new class of N-hydroxycinnam ...
Hordeum vulgare
J. Biol. Chem.
278
13919-13927
2003
2
-
1
-
-
-
4
13
-
-
2
-
-
5
-
-
1
-
-
1
2
1
3
1
1
1
-
-
1
1
-
-
-
-
-
2
-
1
-
-
-
-
-
4
-
13
-
-
2
-
-
-
-
1
-
1
2
1
3
1
1
1
-
-
1
1
-
-
-
-
-
-
-
-
487361
Bird
-
Agmatine coumaroyltransferase ...
Hordeum vulgare
Methods Enzymol.
94
344-347
1983
-
-
-
-
-
-
-
2
-
-
1
-
-
1
-
-
1
-
-
1
1
1
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
1
-
1
1
1
3
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
487362
Bird
-
Agmatine coumaroyltransferase ...
Hordeum vulgare
Phytochemistry
22
2401-2403
1983
-
-
-
-
-
1
-
6
1
-
1
-
-
1
-
-
1
-
-
1
1
-
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
6
1
-
1
-
-
-
-
1
-
1
1
-
6
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
487360
Bird
-
The biosynthesis of coumaroyla ...
Hordeum vulgare
Phytochemistry
20
2345-2346
1981
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
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2
-
1
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1
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1
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1
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2
-
1
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1
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