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
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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
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results (General Information
General Information on EC 4.1.1.25 - tyrosine decarboxylase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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structural basis of the substrate selectivity of enzyme TyDC9, crystal structure analysis, and molecular docking of tyrosine, dopa, tyrosine, tryptophan into the active site and simulation revealing the substrate binding sites and the residues required for conformational stability, active site analysis, overview
evolution
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tyrosine decarboxylase (TyDC) is a member of aromatic amino acid decarboxylases (AAADs), which are a group of phylogenetically diverse enzymes grouped together based on their pyridoxal 5'-phosphate (PLP) dependence and sequence homology. Tyrosine decarboxylase (TyDC) is a type II pyridoxal 5'-phosphate decarboxylase that has a generally high sequence identity to other aromatic amino acid decarboxylases (AAADs)
evolution
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tyrosine decarboxylase (TyDC) is a type II pyridoxal 5'-phosphate decarboxylase and shares high identity with 3,4-dihydroxy-L-phenylalanine (DOPA) decarboxylase (DDC), glutamic acid decarboxylase (GAD), and histidine decarboxylase (HDC). From an evolutionary point of view, the TDC system in Lactobacillus brevis is responsible for tyramine formation in response to acid challenge. The TDC system can generate a proton motive force (PMF) through proton consumption in the decarboxylation reaction and the membrane potential resulting from electrogenic transport of tyrosine in exchange for its corresponding biogenic amine tyramine
malfunction
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Malpighian tubules isolated from Tdc1f03311 homozygous flies show no significant depolarization of their transepithelial potential or diuresis in response to tyrosine while retaining normal sensitivity to tyramine, the null mutant allele of the neuronal TDC isoform Tdc2 has no effect on either tyrosine or tyramine sensitivity
malfunction
the tyrosine modulation over AGDI route is not observed in the mutant 1tdc strain
malfunction
Enterococcus faecalis ATCC 700802 / V583
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the tyrosine modulation over AGDI route is not observed in the mutant 1tdc strain
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metabolism
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changes in the contents of plant biogenic amines (putrescine, cadaverine, spermidine, tryptamine, spermine and histamine) and key enzymes of their biosynthesis, i.e. lysine decarboxylase (LDC), tyrosine decarboxylase, and ornithine decarboxylase (ODC) in galls and other parts of Siberian elm (Ulmus pumila) leaves during the galling process caused by the aphid Tetraneura ulmi, overview
metabolism
relationship among tyrosine decarboxylase and agmatine deiminase pathways in Enterococcus faecalis, the tdc cluster is involved in the tyrosine induction of putrescine biosynthesis, overview
metabolism
Enterococcus faecalis ATCC 700802 / V583
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relationship among tyrosine decarboxylase and agmatine deiminase pathways in Enterococcus faecalis, the tdc cluster is involved in the tyrosine induction of putrescine biosynthesis, overview
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physiological function
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synthesis of tyramine by Tdc1 in the principal cells of the Malpighian tubule is required for physiological responses to tyrosine
physiological function
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alkaloid biosynthesis at early developmental stages is related to embryo growth and development
physiological function
over-expression results in a marked increase of tyrosol and salidroside content in transgenic plants
physiological function
the phenylalanine residue in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing aromaic amino acid decarboxylases
physiological function
Enterococci are considered mainly responsible for the undesirable accumulation of the biogenic amines tyramine and putrescine in cheeses, especially by Enterococcus faecalis. The consumption of foods with high concentrations of tyramine can cause intoxications. Tyramine shows cytotoxicity in vitro and produces necrosis in intestinal cells. Tyramine shows a cytotoxic synergistic effect with histamine, which is also a common biogenic amine in cheeses. Tyramine is formed by the decarboxylation of the amino acid tyrosine, by the tyrosine decarboxylase (TDC) route encoded in the tdc cluster. Tyrosine exerts a role in the maintaining of the pH homeostasis in Enterococcus faecalis. Putrescine is formed from agmatine by the agmatine deiminase (AGDI, EC 3.5.3.12) pathway encoded in the agdi cluster. Tyrosine and agmatine transcriptionally regulate the tdc and agdi clusters. Possible coregulation among TDC and AGDI pathways in Enterococcus faecalis, overview. In the presence of agmatine, a positive correlation between putrescine biosynthesis and the tyrosine concentration occurs, tyrosine induces the transcription of putrescine biosynthesis genes and upregulates pathways involved in cell growth, e.g. the PaguB promoter of agdi catabolic genes. AguR, the transcriptional regulator of agdi, is implicated in interaction among the two clusters. The production of putrescine increases with tyrosine concentration
physiological function
the contents of tyramine lead to flower blotches formation in cyanic blotches of the petals in plant flowers, probably due to the higher expression of VwTYDC gene
physiological function
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the TDC system can generate a proton motive force (PMF) through proton consumption in the decarboxylation reaction and the membrane potential resulting from electrogenic transport of tyrosine in exchange for its corresponding biogenic amine tyramine
physiological function
Enterococcus faecalis ATCC 700802 / V583
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Enterococci are considered mainly responsible for the undesirable accumulation of the biogenic amines tyramine and putrescine in cheeses, especially by Enterococcus faecalis. The consumption of foods with high concentrations of tyramine can cause intoxications. Tyramine shows cytotoxicity in vitro and produces necrosis in intestinal cells. Tyramine shows a cytotoxic synergistic effect with histamine, which is also a common biogenic amine in cheeses. Tyramine is formed by the decarboxylation of the amino acid tyrosine, by the tyrosine decarboxylase (TDC) route encoded in the tdc cluster. Tyrosine exerts a role in the maintaining of the pH homeostasis in Enterococcus faecalis. Putrescine is formed from agmatine by the agmatine deiminase (AGDI, EC 3.5.3.12) pathway encoded in the agdi cluster. Tyrosine and agmatine transcriptionally regulate the tdc and agdi clusters. Possible coregulation among TDC and AGDI pathways in Enterococcus faecalis, overview. In the presence of agmatine, a positive correlation between putrescine biosynthesis and the tyrosine concentration occurs, tyrosine induces the transcription of putrescine biosynthesis genes and upregulates pathways involved in cell growth, e.g. the PaguB promoter of agdi catabolic genes. AguR, the transcriptional regulator of agdi, is implicated in interaction among the two clusters. The production of putrescine increases with tyrosine concentration
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