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Information on EC 2.3.1.64 - agmatine N4-coumaroyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FNP9

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Arabidopsis thaliana
UNIPROT: Q9FNP9 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
atact, agmatine coumaroyltransferase, agmatine coumaryl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agmatine coumaryl transferase
-
agmatine coumaroyltransferase
At5g61160 protein
-
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coumaroyltransferase, agmatine
-
-
-
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p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:agmatine N4-coumaroyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
85030-72-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + agmatine
CoA + 4-coumaroylagmatine
show the reaction diagram
-
-
-
?
feruloyl-CoA + agmatine
CoA + feruloylagmatine
show the reaction diagram
-
-
-
?
feruloyl-CoA + agmatine
CoA + feruloyl agmatine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
feruloyl-CoA + putrescine
CoA + feruloylputrescine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
p-coumaroyl-CoA + agmatine
CoA + p-coumaroylagmatine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
p-coumaroyl-CoA + putrescine
CoA + p-coumaroylputrescine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + agmatine
CoA + 4-coumaroylagmatine
show the reaction diagram
-
-
-
?
feruloyl-CoA + agmatine
CoA + feruloylagmatine
show the reaction diagram
-
-
-
?
feruloyl-CoA + agmatine
CoA + feruloyl agmatine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
feruloyl-CoA + putrescine
CoA + feruloylputrescine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
p-coumaroyl-CoA + agmatine
CoA + p-coumaroylagmatine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
p-coumaroyl-CoA + putrescine
CoA + p-coumaroylputrescine
show the reaction diagram
-
30°C, pH 7.5, pathway analysis with stable isotope-labeled precursors
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
agmatine
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the presence of this substrate inhibits the enzyme reaction with putrescine
enterokinase
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the removal of the thioredoxin domain by enterokinase decreases the enzyme activity but does not alter the relative amounts of products
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p-Coumaroyl-CoA
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the presence of this substrate inhibits the enzyme reaction with feruloyl-CoA
additional information
-
putrescine or feruloyl-CoA do not inhibit the enzyme reaction with agmantine and p-coumaroyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
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with substrates feruloyl-CoA + putrescine 0.0051 nmol feruloylputrescine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
0.000000933
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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
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with substrates feruloyl-CoA + agmatine 2.4 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
0.000112
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with substrates p-coumaroyl-CoA + agmatine 6.7 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
0.000123
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with substrates p-coumaroyl-CoA + agmatine + putrescine 7.4 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30°C, pH 7.5
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cut off rosette leaves infected with the fungus Alternaria brassicicola
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the last reaction of the hydroxycinnamic acid amides biosynthesis
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGCT_ARATH
452
0
51075
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Torenia hybrida
PCR-amplification, expression in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by a combination of jasmonic acid and ethylene. ORA59 binds to the enzyme gene promoter
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 hide
LITERATURE
agriculture
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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.
2
689
2012
Arabidopsis thaliana (Q9FNP9)
Manually annotated by BRENDA team
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.
95
444-457
2018
Arabidopsis thaliana (Q9FNP9), Arabidopsis thaliana
Manually annotated by BRENDA team