2.3.1.110: tyramine N-feruloyltransferase
This is an abbreviated version!
For detailed information about tyramine N-feruloyltransferase, go to the full flat file.
Word Map on EC 2.3.1.110
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2.3.1.110
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amide
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pepper
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potato
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octopamine
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hydroxycinnamic
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plant-specific
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noradrenaline
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l-tyrosine
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capsicum
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annuum
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dopamine
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serotonin
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endosperm-specific
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solanum
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multigene
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4.1.1.25
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syringae
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tuberosum
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tabacum
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elicitor
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xanthi
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cell-suspension
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sinapoyl-coa
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l-phenylalanine
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self-processing
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prolamin
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foot-and-mouth
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4-coumarate:coenzyme
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n-p-coumaroyl
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caffeoyl
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nutrition
- 2.3.1.110
- amide
-
pepper
- potato
- octopamine
-
hydroxycinnamic
-
plant-specific
- noradrenaline
- l-tyrosine
- capsicum
- annuum
- dopamine
- serotonin
-
endosperm-specific
-
solanum
-
multigene
-
4.1.1.25
- syringae
- tuberosum
- tabacum
- elicitor
-
xanthi
-
cell-suspension
- sinapoyl-coa
- l-phenylalanine
-
self-processing
-
prolamin
- foot-and-mouth
-
4-coumarate:coenzyme
-
n-p-coumaroyl
-
caffeoyl
- nutrition
Reaction
Synonyms
AAT1, AT1, feruloyl-CoA tyramine N-feruloyl-CoA transferase, HTH, hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase, synthase, feruloyltyramine, THT, THT1-3, tyramine feruloyltransferase, tyramine N-feruloyl-CoA transferase, tyramine N-hydroxycinnamoyltransferase, tyramine-hydroxycinnamoyl transferase, tyraminehydroxycinnamoyl transferase
ECTree
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Engineering
Engineering on EC 2.3.1.110 - tyramine N-feruloyltransferase
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F145Y
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
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
a series of chimeric genes is constructed by reciprocal exchange of DNA segments between the serotonin N-hydroxycinnamoyltransferase and tyramine N-hydroxycinnamoyltransferase cDNAs. Functional characterization of the recombinant chimeric proteins revealed that the amino acid residues 129 to 165 of serotonin N-hydroxycinnamoyltransferase and the corresponding residues 125 to 160 in tyramine N-hydroxycinnamoyltransferase are critical structural determinants for amine substrate specificity