Information on EC 2.3.1.110 - tyramine N-feruloyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.110
-
RECOMMENDED NAME
GeneOntology No.
tyramine N-feruloyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + tyramine = CoA + N-feruloyltyramine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hydroxycinnamic acid tyramine amides biosynthesis
-
-
suberin monomers biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA:tyramine N-(hydroxycinnamoyl)transferase
Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as donors, and some aromatic amines can act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
128909-19-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
opium poppy
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-
Manually annotated by BRENDA team
maize, cv. Snwodent 108
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
transgenic tomato plants overexpressing tomato hydroxycinnamoyl-CoA:tyramine N-hydroxycinnamoyl transferase THT display enhanced THT gene expression in leaves as compared with wild-type plants. Leaves, flowers and fruits of THT-overexpressing plants show a higher constitutive accumulation of the amide coumaroyltyramine. Feruloyltyramine also accumulates in these tissues. Accumulation of coumaroyltyramine, feruloyltyramine, ctopamine, and noradrenaline hydroxycinnamic acid amides in response to Pseudomonas syringae pv. tomato infection is higher in transgenic plants. Transgenic plants show an enhanced resistance to the bacterial infection. The hydroxycinnamic acid amides accumulation is accompanied by an increase in salicylic acid levels and pathogenesis-related gene induction
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 + octopamine
CoA + N-(4-coumaroyl)octopamine
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + phenethylamine
CoA + N-(4-coumaroyl)phenethylamine
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + tryptamine
CoA + N-(4-coumaroyl)tryptamine
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + tyramine
CoA + N-(4-coumaroyl)tyramine
show the reaction diagram
caffeoyl-CoA + serotonin
CoA + N-caffeoylserotonin
show the reaction diagram
caffeoyl-CoA + tryptamine
CoA + N-caffeoyltryptamine
show the reaction diagram
-
tryptamine at 17% the rate of phenylethylamine
-
-
?
caffeoyl-CoA + tyramine
CoA + N-caffeoyltyramine
show the reaction diagram
cinnamoyl-CoA + tyramine
CoA + cinnamoyltyramine
show the reaction diagram
cinnamoyl-CoA + tyramine
CoA + N-cinnamoyltyramine
show the reaction diagram
-
-
-
?
feruloyl-4'-phosphopantetheine + tyramine
4'-phosphopantetheine + feruloyltyramine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + (4-hydroxyphenyl)propylamine
CoA + feruloyl-(4-hydroxyphenyl)propylamine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + 3'-methoxyoctopamine
CoA + feruloyl-3'-methoxyoctopamine
show the reaction diagram
-
-
-
?
feruloyl-CoA + 3-methoxytyramine
CoA + feruloyl-3-methoxytyramine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + beta-phenylethylamine
CoA + feruloyl-beta-phenylethylamine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + dopamine
CoA + feruloyldopamine
show the reaction diagram
feruloyl-CoA + homotyramine
CoA + feruloylhomotyramine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + N-methyltyramine
CoA + N-feruloyl-N-methyltyramine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + noradrenaline
CoA + feruloylnoradrenaline
show the reaction diagram
feruloyl-CoA + octopamine
CoA + feruloyloctopamine
show the reaction diagram
feruloyl-CoA + phenethylamine
CoA + feruloylphenethylamine
show the reaction diagram
feruloyl-CoA + synephrine
CoA + feruloylsynephrine
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + tryptamine
CoA + feruloyltryptamine
show the reaction diagram
feruloyl-CoA + tyramine
CoA + feruloyltyramine
show the reaction diagram
feruloyl-CoA + tyramine
CoA + N-feruloyltyramine
show the reaction diagram
-
-
-
?
isoferuloyl-CoA + tyramine
CoA + isoferuloyltyramine
show the reaction diagram
-
-
-
-
?
sinapoyl-CoA + tyramine
CoA + sinapoyltyramine
show the reaction diagram
additional information
?
-
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
feruloyl-CoA + tyramine
CoA + feruloyltyramine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
MgCl2 has no influence
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-hydroxyphenyl)amino sulfinyl acetic acid 1,1-dimethyl ester
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i.e. OH-PAS, rapid inhibition, feruloyl-CoA prevents partially
ammonium sulfate
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20% activity at 0.5 M
CuSO4
-
almost complete inactivation at 1 mM
D-tyrosine methyl ester
-
-
diethyldicarbonate
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90% loss of activity after 5 min at 0.5 mM, preincubation with feruloyl-CoA protects
DL-tyrosine methyl ester
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-
FeSO4
-
almost complete inactivation at 1 mM
L-phenylalanine beta-naphthylamide
L-tyrosine 7-amido-4-methylcoumarin
L-tyrosine benzyl ester
L-tyrosine beta-naphthylamide
L-tyrosine ethyl ester
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-
L-tyrosine methyl ester
-
-
L-tyrosine-tert-butyl ester
-
-
L-tyrosineamide
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-
L-tyrosinol
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-
N-ethylmaleimide
N-Methyltyramine
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-
NaCl
-
20% activity at 0.5 M
p-chloromercuribenzoate
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1 mM, strong
tryptamine
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0.1 mM inhibits activity with tyramine
tyramine
ZnCl2
-
almost complete inactivation at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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addition of 14% leads to 2fold increase of enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.585
3-methoxytyramine
-
-
0.002 - 0.3
4-Coumaroyl-CoA
0.17
4-hydroxyphenylpropylamine
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-
4.276
beta-phenylethylamine
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-
0.0127 - 0.326
caffeoyl-CoA
0.002 - 0.49
cinnamoyl-CoA
0.078 - 0.779
dopamine
0.0125
feruloyl-4'-phosphopantetheine
-
-
-
0.0006 - 0.192
Feruloyl-CoA
0.002
isoferuloyl-CoA
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-
1.57
noradrenaline
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-
0.0113
octopamine
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-
0.0067
p-Coumaroyl-CoA
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+ tyramine
0.112 - 0.57
phenethylamine
1.389
Phenylethylamine
-
pH 8.5, 30C
0.073 - 25.44
serotonin
0.001 - 0.05
Sinapoyl-CoA
0.059 - 24
tryptamine
0.0043 - 1.165
tyramine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58
D-tyrosine methyl ester
-
-
0.055
DL-tyrosine methyl ester
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-
0.091 - 0.112
L-phenylalanine beta-naphthylamide
0.00042 - 0.00072
L-tyrosine 7-amido-4-methylcoumarin
0.003 - 0.0034
L-tyrosine benzyl ester
0.0003 - 0.00066
L-tyrosine beta-naphthylamide
0.02
L-tyrosine ethyl ester
-
-
0.026
L-tyrosine methyl ester
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-
0.018
L-tyrosine-tert-butyl ester
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2
L-tyrosineamide
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-
0.046
L-tyrosinol
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2.2
N-Methyltyramine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.132
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 8
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optimum varies slightly between different fractions
8
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sinapoyl-CoA
8.5
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cinnamoyl-CoA
9
-
p-coumaroyl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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formation of feruloyltyramine, half-maximal activity at pH 6.5 and pH 9.0
6.5 - 9.5
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half-maximal activity at pH 6.5 and pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
THT mRNA is expressed constitutively in all pepper organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
SDS-PAGE
26000
-
calculated from amino acid sequence
28220
-
calculated from amino acid sequence
28400
-
calculated from amino acid sequence
30000
-
SDS-PAGE
40000
-
gel filtration
45000
-
gel filtration
48000
-
gel filtration
50000
-
gel filtration
55000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 28221, calculatred from nucleotide sequence
monomer
1 * 50600, about, LAAT1, sequence determination
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10% glycerol in liquid N2 stabilizes
-
freezing does not alter the properties of the enzyme
-
no loss of activity during dialysis for 16 h at 4C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
O2-sensitive
-
486127
O2-sensitive, mercaptoethanol stabilizes, crude extract
-
486126
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, no loss of activity for 2 months in the presence of 2-mercaptoethanol
-
-80C, no loss of activity for 4 months in the presence of 2-mercaptoethanol
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4C, 10% loss of activity within 7 days, concentrated enzyme
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4C, as ammonium sulfate paste, 10 mM mercaptoethanol, 24 h, 25% loss of activity
-
4C, as ammonium sulfate paste, 5 mM DTT, 10% loss of activity within 24 h
-
4C, no loss of activity for 14 days in the presence of 2-mercaptoethanol
-
4C, purified recombinant GST-tagged AAT1, in 50 mM Tris-Cl, pH 8.0, and 10 mM reduced glutathione, 4 weeks, stable
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
46fold, separation of 3 fractions with different specificities
-
homogeneity
-
partial
recombinant GST-tagged AAT1 from Escherichia coli by cell disruption through freeze-thaw cycles, and glutathione affinity chromatography
recombinant protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AAT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree of BAHD acyltransferases, expression of GST-tagged AAT1 in Escherichia coli strain Rosetta(DE3)pLysS
expression in Escherichia coli
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transformation of fusion product of THT and tyrosine decarboxylase in Agrobacterium tumefaciens
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F145Y
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KM-value for tyramine is 2.3fold lower than wild-type value, Vmax is 3fold lower than wild-type value. Wild-type enzyme shows no activity with serotonin, mutant enzyms shows activity with serotonin
F145Y/Y147F
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KM-value for tyramine is 2.3fold lower than wild-type value, Vmax is 4.2fold lower than wild-type value. Wild-type enzyme shows no activity with serotonin, mutant enzyms shows activity with serotonin
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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production of plant secondary metabolites