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Information on EC 4.1.1.25 - tyrosine decarboxylase and Organism(s) Enterococcus faecalis and UniProt Accession Q838D6

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.25 tyrosine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
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This record set is specific for:
Enterococcus faecalis
UNIPROT: Q838D6
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The taxonomic range for the selected organisms is: Enterococcus faecalis
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
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L-tyrosine
=
tyramine
+
CO2
=
+
Synonyms
tdc, tyrosine decarboxylase, l-amino acid decarboxylase, tyrdc, l-tyrosine decarboxylase, tydc1, tyrosine/dopa decarboxylase, dtdc2, vwtydc, tyr decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tyrosine decarboxylase
-
Decarboxylase, tyrosine
-
-
-
-
ELI5
-
-
-
-
L-(-)-Tyrosine apodecarboxylase
-
-
-
-
L-Tyrosine decarboxylase
-
-
-
-
TYDC/DODC
-
-
-
-
Tyrosine/Dopa decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9002-09-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Tyrosine
Tyramine + CO2
show the reaction diagram
-
-
-
?
L-phenylalanine
beta-phenylethylamine + CO2
show the reaction diagram
L-Tyr
Tyramine + CO2
show the reaction diagram
L-Tyrosine
Tyramine + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Tyrosine
Tyramine + CO2
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-Fluoromethyl(3,4-dihydroxyphenyl)alanine
-
-
alpha-Fluoromethyltyrosine
-
-
NaCl
decarboxylation of substrate phenylalanine is inhibited increasing concentrations of NaCl, no inhibition for substrate tyrosine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.355 - 1.5
L-Tyr
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the tyrosine modulation over AGDI route is not observed in the mutant 1tdc strain
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70010
-
MALDI TOF mass spectrometry
70053
x * 70053, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70053, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tdcA, genetic organization
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
tdc and agdi cluster genes are induced by tyrosine addition, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allenmark, S.; Servenius, B.
Characterization of bacterial L(-)-tyrosine decarboxylase by isoelectric focusing and gel chromatography
J. Chromatogr.
153
239-245
1978
Enterococcus faecalis
-
Manually annotated by BRENDA team
Phan, A.P.H.; Ngo, T.T.; Lenhoff, H.M.
Tyrosine decarboxylase. Spectrophotometric assay and application in determining pyridoxal-5'-phosphate
Appl. Biochem. Biotechnol.
8
127-133
1983
Enterococcus faecalis
Manually annotated by BRENDA team
Chapple, C.C.S.; Walker, M.A.; Ellis, B.E.
Plant tyrosine decarboxylase can be strongly inhibited by L-alpha-aminooxy-beta-phenylpropionate
Planta
167
101-105
1986
Enterococcus faecalis, Hordeum vulgare, Nicotiana tabacum, Sanguinaria canadensis, Syringa vulgaris
Manually annotated by BRENDA team
Pamuk, F.
Investigation of some properties and glycine inhibition of L-tyrosine decarboxylase from S. faecalis by a pCO2 membrane electrode
Commun. Fac. Sci. Univ. Ank. Ser. C
35
103-114
1989
Enterococcus faecalis
-
Manually annotated by BRENDA team
Komprda, T.; Burdychova, R.; Dohnal, V.; Cwikova, O.; Sladkova, P.; Dvorackova, H.
Tyramine production in Dutch-type semi-hard cheese from two different producers
Food Microbiol.
25
219-227
2008
Enterococcus faecalis, Latilactobacillus curvatus, Enterococcus durans, Enterococcus casseliflavus
Manually annotated by BRENDA team
Torriani, S.; Gatto, V.; Sembeni, S.; Tofalo, R.; Suzzi, G.; Belletti, N.; Gardini, F.; Bover-Cid, S.
Rapid detection and quantification of tyrosine decarboxylase gene (tdc) and its expression in Gram-positive bacteria associated with fermented foods using PCR-based methods
J. Food Prot.
71
93-101
2008
Enterococcus faecalis, Levilactobacillus brevis, Limosilactobacillus fermentum, Latilactobacillus curvatus, Staphylococcus epidermidis, Staphylococcus xylosus, Enterococcus faecalis EF37
Manually annotated by BRENDA team
Pessione, E.; Pessione, A.; Lamberti, C.; Coisson, D.J.; Riedel, K.; Mazzoli, R.; Bonetta, S.; Eberl, L.; Giunta, C.
First evidence of a membrane-bound, tyramine and beta-phenylethylamine producing, tyrosine decarboxylase in Enterococcus faecalis: a two-dimensional electrophoresis proteomic study
Proteomics
9
2695-2710
2009
Enterococcus faecalis, Enterococcus faecalis DISAV1022
Manually annotated by BRENDA team
Liu, F.; Xu, W.; Du, L.; Wang, D.; Zhu, Y.; Geng, Z.; Zhang, M.; Xu, W.
Heterologous expression and characterization of tyrosine decarboxylase from Enterococcus faecalis R612Z1 and Enterococcus faecium R615Z1
J. Food Prot.
77
592-598
2014
Enterococcus faecium, Enterococcus faecalis (Q8KXD2), Enterococcus faecalis R612Z1 (Q8KXD2), Enterococcus faecalis R612Z1, Enterococcus faecium R615Z1
Manually annotated by BRENDA team
Perez, M.; Ladero, V.; Del Rio, B.; Redruello, B.; de Jong, A.; Kuipers, O.; Kok, J.; Martin, M.C.; Fernandez, M.; Alvarez, M.A.
The relationship among tyrosine decarboxylase and agmatine deiminase pathways in Enterococcus faecalis
Front. Microbiol.
8
2107
2017
Enterococcus faecalis (Q838D6), Enterococcus faecalis ATCC 700802 / V583 (Q838D6)
Manually annotated by BRENDA team