Information on EC 2.3.1.64 - agmatine N4-coumaroyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.64
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RECOMMENDED NAME
GeneOntology No.
agmatine N4-coumaroyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-coumaroyl-CoA + agmatine = CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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hordatine biosynthesis
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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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
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
caffeoyl-CoA + agmatine
CoA + caffeoylagmatine
show the reaction diagram
cinnamoyl-CoA + agmatine
CoA + cinnamoyl agmatine
show the reaction diagram
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-
-
?
feruloyl-CoA + agmatine
CoA + feruloyl agmatine
show the reaction diagram
feruloyl-CoA + putrescine
CoA + feruloylputrescine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
p-coumaroyl-CoA + agmatine
CoA + p-coumaroylagmatine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
p-coumaroyl-CoA + putrescine
CoA + p-coumaroylputrescine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
sinapoyl-CoA + agmatine
CoA + sinapoyl agmatine
show the reaction diagram
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-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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reaction in hordatine anabolism
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?
feruloyl-CoA + agmatine
CoA + feruloyl agmatine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
feruloyl-CoA + putrescine
CoA + feruloylputrescine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
p-coumaroyl-CoA + agmatine
CoA + p-coumaroylagmatine
show the reaction diagram
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30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
p-coumaroyl-CoA + putrescine
CoA + p-coumaroylputrescine
show the reaction diagram
-
30C, pH 7.5, pathway analysis with stable isotope-labeled precursors
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-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
agmatine
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the presence of this substrate inhibits the enzyme reaction with putrescine
CuSO4
10 mM, 85% inhibition
dithiothreitol
30% inhibition
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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MnCl2
10 mM, 29% inhibition
p-Coumaroyl-CoA
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the presence of this substrate inhibits the enzyme reaction with feruloyl-CoA
ZnSO4
10 mM, 99% inhibition
additional information
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putrescine or feruloyl-CoA do not inhibit the enzyme reaction with agmantine and p-coumaroyl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-mercapto-2,3-propanediol
1 mM is required for optimal activity
2-mercaptoethanol
1 mM is required for optimal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00074 - 0.0021
4-Coumaroyl-CoA
0.0052 - 0.012
agmatine
0.0033 - 0.0058
caffeoyl-CoA
0.0033
cinnamoyl-CoA
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0.0013 - 0.0066
Feruloyl-CoA
0.05
Sinapoyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000003
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with substrates p-coumaroyl-CoA + agmatine + putrescine 0.0018 nmol coumaroylputrescine/mg/protein/h, recombinant enzyme, 30C, pH 7.5
0.000000085
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with substrates feruloyl-CoA + putrescine 0.0051 nmol feruloylputrescine/mg/protein/h, recombinant enzyme, 30C, 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, 30C, pH 7.5
0.00002
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with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 1.2 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30C, pH 7.5
0.00004
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with substrates feruloyl-CoA + agmatine 2.4 nmol feruloylagmatine/mg/protein/h, recombinant enzyme, 30C, 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, 30C, 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, 30C, pH 7.5
0.000187
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with substrates p-coumaroyl-CoA + feruloyl-CoA + agmatine 11.2 nmol p-coumaroylagmatine/mg/protein/h, recombinant enzyme, 30C, pH 7.5
11.34
recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 8.1
half-maximal activity at pH 6.9 and pH 8.1
7 - 8
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approx. half-maximal activity at pH 7.0 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cut off rosette leaves infected with the fungus Alternaria brassicicola
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
1 * 48000, SDS-PAGE
70000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 48000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40C, concentrated preparation at least 1 month, negligible loss of activity
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0C, 100 mM Tris, pH 7.5, 1 mM EDTA, 10 mM 2-mercaptoethanol, 50 mM KCl
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Biogel A, Sepharose 4B-agmatine
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Torenia hybrida
PCR-amplification, expression in Escherichia coli BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
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
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