4.1.1.25: tyrosine decarboxylase
This is an abbreviated version!
For detailed information about tyrosine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.25
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4.1.1.25
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children
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autism
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catheter
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taurodeoxycholate
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biogenic
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tunnel
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thyroglossal
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dopamine
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roseus
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faecalis
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catharanthus
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dielectric
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hemodialysis
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lymphedema
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tryptamine
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l-dopa
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taurocholate
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decarboxylases
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forearm
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midline
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arteriovenous
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aadcs
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enterococci
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5-hydroxytryptophan
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octopamine
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strictosidine
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curvatus
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hyoid
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taurochenodeoxycholate
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subdural
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vindoline
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cheeses
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pharmacology
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nephrologists
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inattention
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fpgas
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tauroursodeoxycholate
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catheter-related
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glycocholate
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resting-state
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agriculture
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synthesis
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food industry
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nutrition
- 4.1.1.25
- children
-
autism
-
catheter
- taurodeoxycholate
-
biogenic
-
tunnel
-
thyroglossal
- dopamine
- roseus
- faecalis
- catharanthus
-
dielectric
-
hemodialysis
- lymphedema
- tryptamine
- l-dopa
- taurocholate
- decarboxylases
-
forearm
-
midline
-
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
Reaction
Synonyms
AADC, AtTYDC, Bradi2g51170, Decarboxylase, tyrosine, dTdc1, dTdc2, ELI5, L-(-)-Tyrosine apodecarboxylase, L-amino acid decarboxylase, L-Tyrosine decarboxylase, LbTDC, LOC100840315, MfnA protein, P0665A11.14, PcTYDC2, PF1159, PsTYDC1, PsTYDC2, TDC, tdcA, TYDC, TYDC/DODC, TYDC1, Tydc9, TYR decarboxylase, TyrDC, TyrDC-2, tyrosine decarboxylase, tyrosine decarboxylase-2, Tyrosine/Dopa decarboxylase, tyrosine/Dopa decarboxylase-1, tyrosine/Dopa decarboxylase-2, VwTYDC
ECTree
4.1.1.25 tyrosine decarboxylaseAdvanced search results
results (
results (Engineering
Engineering on EC 4.1.1.25 - tyrosine decarboxylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
E102A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
E299A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
G296F
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
H241N
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site-directed saturation mutagenesis, almost inactive mutant
H241Q
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site-directed saturation mutagenesis, almost inactive mutant
H391A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
H98A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
K240A
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site-directed saturation mutagenesis, the mutant shows 36% reduced catalytic efficiency compared to wild-type
M505A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
M588A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
M99A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
N100A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
P397A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S101A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S297A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S586A
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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
S586E
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site-directed saturation mutagenesis, almost inactive mutant
S586F
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site-directed saturation mutagenesis, almost inactive mutant
S586G
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
S586I
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site-directed saturation mutagenesis, almost inactive mutant
S586L
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site-directed saturation mutagenesis, almost inactive mutant
S586T
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site-directed saturation mutagenesis, the mutant highly shows reduced activity compared to wild-type
S586V
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site-directed saturation mutagenesis, the mutant highly shows reduced activity compared to wild-type
T103A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
T298A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
V294A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
V396A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y331A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y395A
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site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type
Y398A
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site-directed saturation mutagenesis, almost inactive mutant
Y398F
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site-directed saturation mutagenesis, the mutant shows highly reduced activity compared to wild-type
F346Y
alteration in the primary activity from decarboxylation-deamination to decarboxylation. Mutant retains a small percentage of decarboxylation-deamination activity
additional information
additional information
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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
Enterococcus faecalis ATCC 700802 / V583
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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
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additional information
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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
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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
