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2-fluoro-L-tyrosine
2-fluorotyramine + CO2
-
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
L-aspartate
3-aminopropionic acid + CO2
95% of the activity with L-tyrosine
-
-
?
L-glutamate
4-aminobutyric acid + CO2
80% of the activity with L-tyrosine
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
L-phenylalanine + H2O
phenylethylamine + H2O2
-
reaction of mutant F338Y
-
?
L-Tyrosine
Tyramine + CO2
L-tyrosine + H2O
4-hydroxyphenylacetaldehyde + CO2 + NH3
-
enzyme catalyzes decarboxylation and subsequent deamination of substrate
-
?
additional information
?
-
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
-
-
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
Thalictrum rugosum
-
at 74% of the activity with L-Tyr
-
-
?
L-Dopa
dopamine + CO2
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
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
-
?
L-Dopa
dopamine + CO2
43.9% of the activity with L-tyrosine
-
-
?
L-Dopa
dopamine + CO2
-
shows about half of the catalytic efficiency compared to L-tyrosine
-
-
?
L-Dopa
dopamine + CO2
43.9% of the activity with L-tyrosine
-
-
?
L-Dopa
dopamine + CO2
-
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
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
-
?
L-Dopa
dopamine + CO2
-
recombinant TyrDC-2, 19-28% of the specific activity with tyrosine
-
?
L-Dopa
dopamine + CO2
-
the enzyme is involved in decarboxylation of L-Dopa. L-Dopa decarboxylation activity of tyrosine decarboxylase is differentially regulated in response to stress conditions
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
-
-
-
?
L-Dopa
dopamine + CO2
Thalictrum rugosum
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
L-phenylalanine is decarboxylated to beta-phenylethylamine (10% yield) only when tyrosine is completely depleted
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
L-phenylalanine is decarboxylated to beta-phenylethylamine (10% yield) only when tyrosine is completely depleted
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
-
-
-
?
L-Tyr
?
-
catalyzes an early step in the biosynthesis of isoquinoline alkaloids
-
-
?
L-Tyr
?
-
possibly involved in the pathway of salidroside formation
-
-
?
L-Tyr
?
Thalictrum rugosum
-
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
-
-
?
L-Tyr
?
Thalictrum rugosum
-
induced with a yeast polysaccharide preparation, elicitor
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
-
-
-
?
L-Tyr
Tyramine + CO2
Thalictrum rugosum
-
-
-
?
L-Tyr
Tyramine + CO2
Thalictrum rugosum
-
-
-
?
L-Tyr
Tyramine + CO2
Thalictrum rugosum
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
?
L-Tyrosine
Tyramine + CO2
the recombinant protein refuses all other substrates other than L-tyrosine, suggesting TyrDC to be a specific L-tyrosine decarboxylase
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
Citrus sp.
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
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
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
preferred substrate
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
preferred substrate
-
-
?
L-Tyrosine
Tyramine + CO2
-
preferred substrate
-
-
?
L-Tyrosine
Tyramine + CO2
-
preferred substrate
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
preferred substrate
-
-
?
L-Tyrosine
Tyramine + CO2
specific for tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
highly specific for L-tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
preference of L-tyrosine over L-DOPA as substrate
-
?
L-Tyrosine
Tyramine + CO2
-
tyrosine decarboxylation in lactobacilli
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
highly specific for L-tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
tyrosine decarboxylation in lactobacilli
-
?
L-Tyrosine
Tyramine + CO2
-
-
?
L-Tyrosine
Tyramine + CO2
specific for tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
16times higher affinity for tyrosine than for DOPA
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
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
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
Q6BD07
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
?
L-Tyrosine
Tyramine + CO2
-
specific for tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
very substrate-specific
-
?
L-Tyrosine
Tyramine + CO2
-
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
-
?
L-Tyrosine
Tyramine + CO2
-
ramification of the shikimate pathway
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
specific for tyrosine
-
?
L-Tyrosine
Tyramine + CO2
-
ramification of the shikimate pathway
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
recombinant TyrDC-2, highest specific activity with tyrosine as substrate
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
the enzyme also catalyzes the decarboxylation of L-glutamate and L-asparate with higher efficiency. No activity with D-tyrosine
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
L-Tyrosine
Tyramine + CO2
Thalictrum rugosum
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
-
?
L-Tyrosine
Tyramine + CO2
-
-
-
?
additional information
?
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
not: histidine, lysine, phenylalanine, tryptophan, ornithine
-
?
additional information
?
-
-
not: histidine, lysine, phenylalanine, tryptophan, ornithine, L-DOPA
-
?
additional information
?
-
-
agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus, overview
-
-
?
additional information
?
-
no substrates: L-phenylalanine, L-tryptophan
-
-
?
additional information
?
-
-
no substrates: L-phenylalanine, L-tryptophan
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
no substrates: L-phenylalanine, L-tryptophan
-
-
?
additional information
?
-
-
agmatine deiminase pathway genes in Lactobacillus brevis are linked to the tyrosine decarboxylation operon in a putative acid resistance locus, overview
-
-
?
additional information
?
-
-
not: histidine, lysine, phenylalanine, tryptophan, ornithine, L-DOPA
-
?
additional information
?
-
-
not: 5-hydroxytryptophan
-
?
additional information
?
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
not: tryptophan
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
not: tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
no substrate: L-tryptophan
-
-
?
additional information
?
-
-
no substrate: L-tryptophan
-
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
-
exclusive substrate specificity for L-amino acids with either indole or phenol side chains, but not both, inactive toward L-phenylalanine and L-tryptophan
-
?
additional information
?
-
Thalictrum rugosum
-
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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F338Y
alteration in the primary activity from decarboxylation/deamination to decarboxylation. Mutant displays a very low activity to tyrosine, i.e. about 5% of its activity to phenylalanine, and strong activity to DOPA
A295F
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
E102A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
E299A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
G296F
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
H241N
-
site-directed saturation mutagenesis, almost inactive mutant
H241Q
-
site-directed saturation mutagenesis, almost inactive mutant
H391A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
H98A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
K240A
-
site-directed saturation mutagenesis, the mutant shows 36% reduced catalytic efficiency compared to wild-type
M505A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
M588A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
M99A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
N100A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
P397A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S101A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S297A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S586A
-
site-directed saturation mutagenesis, the mutant variant displays 278% of the catalytic efficiency of the wild-type and increased substrate affinity, which is attributed to decreased steric hindrance and increased hydrophobicity
S586C
-
site-directed saturation mutagenesis, inactive mutant
S586D
-
site-directed saturation mutagenesis, inactive mutant
S586E
-
site-directed saturation mutagenesis, almost inactive mutant
S586F
-
site-directed saturation mutagenesis, almost inactive mutant
S586G
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S586H
-
site-directed saturation mutagenesis, inactive mutant
S586I
-
site-directed saturation mutagenesis, almost inactive mutant
S586K
-
site-directed saturation mutagenesis, inactive mutant
S586L
-
site-directed saturation mutagenesis, almost inactive mutant
S586M
-
site-directed saturation mutagenesis, inactive mutant
S586N
-
site-directed saturation mutagenesis, inactive mutant
S586P
-
site-directed saturation mutagenesis, inactive mutant
S586Q
-
site-directed saturation mutagenesis, inactive mutant
S586R
-
site-directed saturation mutagenesis, inactive mutant
S586T
-
site-directed saturation mutagenesis, the mutant highly shows reduced activity compared to wild-type
S586V
-
site-directed saturation mutagenesis, the mutant highly shows reduced activity compared to wild-type
S586W
-
site-directed saturation mutagenesis, inactive mutant
S586Y
-
site-directed saturation mutagenesis, inactive mutant
T103A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
T298A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
V294A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
V396A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y331A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y395A
-
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y398A
-
site-directed saturation mutagenesis, almost inactive mutant
Y398F
-
site-directed saturation mutagenesis, the mutant shows highly reduced activity compared to wild-type
Y420A
-
site-directed mutagenesis, inactive mutant
Y420F
-
site-directed mutagenesis, inactive mutant
F346Y
alteration in the primary activity from decarboxylation-deamination to decarboxylation. Mutant retains a small percentage of decarboxylation-deamination activity
additional information
-
the mutant allele of Tdc1, Tdc1f03311, reduces expression of the mature Tdc1 transcript by greater than 100fold
additional information
construction of enzyme knockout mutant strain V583 DELTAtdc, a non-tyramine-producing mutant that lacks the decarboxylase genes cluster. Gene expression of aguA gene is measured by quantitative RT-PCR in cultures of the wild-type and DELTAtdc knockout mutant strains
additional information
-
construction of enzyme knockout mutant strain V583 DELTAtdc, a non-tyramine-producing mutant that lacks the decarboxylase genes cluster. Gene expression of aguA gene is measured by quantitative RT-PCR in cultures of the wild-type and DELTAtdc knockout mutant strains
-
additional information
-
structure-guided site-directed mutagenesis and alanine scanning and saturation mutagenesis of LbTDC are performed on residues around the substrate binding sites and those required for conformational stability to elucidate the function of key residues involved in the catalytic mechanism and to promote the potential applications of LbTDC in tyramine synthesis, food safety, and pharmacology
additional information
-
fusion construct of tyrosine decarboxylase and tyramine N-hydroycinnamoyltransferase
additional information
generation of a chimeric protein composed of Thalictrum flavum tyrosine decarboxylase residues 1300 and Petroselinum crispum romatic acetaldehyde synthase residues 300514. The hybrid enzyme behaves primarily as a wild-type Petroselinum crispum acetaldehyde synthase
additional information
generation of a chimeric protein composed of Thalictrum flavum tyrosine decarboxylase residues 1300 and Petroselinum crispum romatic acetaldehyde synthase residues 300514. The hybrid enzyme behaves primarily as a wild-type Petroselinum crispum acetaldehyde synthase
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Allenmark, S.; Servenius, B.
Characterization of bacterial L(-)-tyrosine decarboxylase by isoelectric focusing and gel chromatography
J. Chromatogr.
153
239-245
1978
Enterococcus faecalis
-
brenda
Phan, A.P.H.; Ngo, T.T.; Lenhoff, H.M.
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