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Information on EC 4.1.1.25 - tyrosine decarboxylase
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4.1.1.25 tyrosine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
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Word Map
- 4.1.1.25
- children
-
autism
-
catheter
- taurodeoxycholate
-
biogenic
-
tunnel
-
thyroglossal
- dopamine
- roseus
- faecalis
- catharanthus
-
dielectric
-
hemodialysis
- lymphedema
- tryptamine
- l-dopa
- taurocholate
- decarboxylases
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forearm
-
midline
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arteriovenous
-
aadcs
-
enterococci
- 5-hydroxytryptophan
- octopamine
- strictosidine
- curvatus
-
hyoid
- taurochenodeoxycholate
-
subdural
- vindoline
-
cheeses
- pharmacology
-
nephrologists
-
inattention
-
fpgas
- tauroursodeoxycholate
-
catheter-related
- glycocholate
-
resting-state
- agriculture
- synthesis
- food industry
- nutrition
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
tdc, tyrosine decarboxylase, l-amino acid decarboxylase, tyrdc, l-tyrosine decarboxylase, tydc1, dtdc2, tyrosine/dopa decarboxylase, vwtydc, tyr decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AADC
Decarboxylase, tyrosine
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ELI5
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L-(-)-Tyrosine apodecarboxylase
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L-amino acid decarboxylase
L-Tyrosine decarboxylase
TDC
tdcA
TYDC
TYDC/DODC
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TyrDC
tyrosine decarboxylase
Tyrosine/Dopa decarboxylase
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L-Tyrosine decarboxylase
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TDC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tyrosine = tyramine + CO2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine carboxy-lyase (tyramine-forming)
A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
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CAS REGISTRY NUMBER
COMMENTARY
9002-09-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate
3-aminopropionic acid + CO2
95% of the activity with L-tyrosine
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?
L-glutamate
4-aminobutyric acid + CO2
80% of the activity with L-tyrosine
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-
?
L-phenylalanine + H2O
phenylethylamine + H2O2
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reaction of mutant F338Y
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?
L-tyrosine + H2O
4-hydroxyphenylacetaldehyde + CO2 + NH3
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enzyme catalyzes decarboxylation and subsequent deamination of substrate
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?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
Thalictrum rugosum
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at 74% of the activity with L-Tyr
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-
?
L-Dopa
dopamine + CO2
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preference of L-tyrosine over L-DOPA as substrate, strain IOEB 9809: 18% of activity of L-tyrosine decarboxylation, strain ATCC 367: 22% of activity of L-tyrosine decarboxylation
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?
L-Dopa
dopamine + CO2
43.9% of the activity with L-tyrosine
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?
L-Dopa
dopamine + CO2
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shows about half of the catalytic efficiency compared to L-tyrosine
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?
L-Dopa
dopamine + CO2
Levilactobacillus brevis CGMCC 1.2028
43.9% of the activity with L-tyrosine
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-
?
L-Dopa
dopamine + CO2
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16times lower affinity for DOPA than for tyrosine, the decarboxylation of DOPA is inhibited in the presence of the cofactor pyridoxal 5-phosphate by 50-60%, maximum activity towards DOPA in the absence of the cofactor
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?
L-Dopa
dopamine + CO2
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recombinant TyrDC-2, 19-28% of the specific activity with tyrosine
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?
L-Dopa
dopamine + CO2
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the enzyme is involved in decarboxylation of L-Dopa. L-Dopa decarboxylation activity of tyrosine decarboxylase is differentially regulated in response to stress conditions
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-
?
L-phenylalanine
beta-phenylethylamine + CO2
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L-phenylalanine is decarboxylated to beta-phenylethylamine (10% yield) only when tyrosine is completely depleted
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?
L-phenylalanine
beta-phenylethylamine + CO2
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L-phenylalanine is decarboxylated to beta-phenylethylamine (10% yield) only when tyrosine is completely depleted
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?
L-Tyr
?
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catalyzes an early step in the biosynthesis of isoquinoline alkaloids
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?
L-Tyr
?
Thalictrum rugosum
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inducible in late exponential and early stationary growth phases, induced by treatment with yeast glucan elicitor, may be a key enzyme between primary and secondary metabolisms in the biosynthesis of norlaudanosoline-derived alkaloids
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-
?
L-Tyrosine
Tyramine + CO2
the recombinant protein refuses all other substrates other than L-tyrosine, suggesting TyrDC to be a specific L-tyrosine decarboxylase
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-
?
L-Tyrosine
Tyramine + CO2
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flies with a mutation in dTdc2 lack neural tyramine and octopamine and are female sterile due to egg retention. Dtdc2 mutants release eggs into the oviducts but are unable to deposit them
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?
L-Tyrosine
Tyramine + CO2
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highly specific for L-tyrosine
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?
L-Tyrosine
Tyramine + CO2
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preference of L-tyrosine over L-DOPA as substrate
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?
L-Tyrosine
Tyramine + CO2
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tyrosine decarboxylation in lactobacilli
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?
L-Tyrosine
Tyramine + CO2
Levilactobacillus brevis IOEB 9809
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tyrosine decarboxylation in lactobacilli
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?
L-Tyrosine
Tyramine + CO2
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16times higher affinity for tyrosine than for DOPA
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?
L-Tyrosine
Tyramine + CO2
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under some circumstances, enzyme activity can exert a rate-limiting control over the carbon flux allocated to the biosynthesis of hydroxycinnamic acid amides of tyramine
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?
L-Tyrosine
Tyramine + CO2
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first enzyme in poppy alkaloid biosynthesis, first biosynthetic step in the tetrahydroisoquinoline pathway, TyDC serves as a channel between the aromatic amino acids L-thyrosine and L-dopa and the biosynthesis of all of the opium poppy alkaloids
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?
L-Tyrosine
Tyramine + CO2
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ramification of the shikimate pathway
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?
L-Tyrosine
Tyramine + CO2
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ramification of the shikimate pathway
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?
L-Tyrosine
Tyramine + CO2
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recombinant TyrDC-2, highest specific activity with tyrosine as substrate
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?
L-Tyrosine
Tyramine + CO2
the enzyme also catalyzes the decarboxylation of L-glutamate and L-asparate with higher efficiency. No activity with D-tyrosine
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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not: histidine, lysine, phenylalanine, tryptophan, ornithine
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?
additional information
?
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not: histidine, lysine, phenylalanine, tryptophan, ornithine, L-DOPA
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?
additional information
?
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agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus, overview
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?
additional information
?
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no substrates: L-phenylalanine, L-tryptophan
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?
additional information
?
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no substrates: L-phenylalanine, L-tryptophan
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?
additional information
?
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key residues involved in conformational swing and substrate binding, e.g. H241, K240, or S586, molecular docking and mutational analysis, overview. Residue S586 is a critical residue for substrate binding
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?
additional information
?
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Levilactobacillus brevis CGMCC 1.2028
no substrates: L-phenylalanine, L-tryptophan
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?
additional information
?
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Levilactobacillus brevis IOEB 9809
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agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus, overview
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?
additional information
?
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Levilactobacillus brevis IOEB 9809
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not: histidine, lysine, phenylalanine, tryptophan, ornithine, L-DOPA
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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TDC catalyzes the decarboxylation of tryptophan to tryptamine and 5-hydroxytryptophan to serotonin. Tryptophan is a good ligand showing the highest binding affinity. Tyrosine and dopa show the same binding affinity only slightly lower as tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
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?
additional information
?
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exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?