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Information on EC 4.1.1.25 - tyrosine decarboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8RY79

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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:
Arabidopsis thaliana
UNIPROT: Q8RY79
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Word Map
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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, tyr decarboxylase, vwtydc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-amino acid decarboxylase
-
Decarboxylase, tyrosine
-
-
-
-
ELI5
-
-
-
-
L-(-)-Tyrosine apodecarboxylase
-
-
-
-
L-Tyrosine decarboxylase
-
-
-
-
TDC
-
-
-
-
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-Dopa
dopamine + CO2
show the reaction diagram
-
-
?
L-phenylalanine + H2O
phenylethylamine + H2O2
show the reaction diagram
-
reaction of mutant F338Y
-
?
L-Tyrosine
Tyramine + CO2
show the reaction diagram
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
-
?
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6 - 5.1
L-phenylalanine
0.745
L-tyrosine
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAAS_ARATH
490
0
54423
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
232000
His-tagged enzyme, non-denaturing blue native gel electrophoresis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 65000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
at pH values above 9.5 the enzymatic activity rapidly declines
703710
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
at temperatures above 60°C protein activity sharply declines
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tagged enzyme in Escherichia coli strain M15
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
heat and cold stress, as well as stimulation by pathogens trigger no significant alteration of TyrDC transcripts
salt stress gives rise to a transient decrease of TyrDC mRNA levels by approximately 50% after 60 min
TyrDC transcription strongly responds to wounding, TyrDC levels peak within 30 min and transcript levels decline thereafter. TyrDC is rapidly activated by drought stress, reaching maximum levels after 60 min
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
biosynthesis of pharmaceutically important monoterpenoid indole alkaloids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Facchini, P.J.; Huber-Allanach, K.L.; Tari, L.W.
Plant aromatic L-amino acid decarboxylases: evolution, biochemistry, regulation, and metabolic engineering applications
Phytochemistry
54
121-138
2000
Chondrodendron tomentosum, Cytisus scoparius, Eschscholzia californica, Hordeum vulgare, Petroselinum crispum, Petunia sp., Sanguinaria canadensis, Syringa vulgaris, Thalictrum rugosum, Colchicum autumnale, Papaver somniferum (P54768), Arabidopsis thaliana (Q8RY79)
Manually annotated by BRENDA team
Lehmann, T.; Pollmann, S.
Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana
FEBS Lett.
583
1895-1900
2009
Arabidopsis thaliana (Q8RY79), Arabidopsis thaliana
Manually annotated by BRENDA team
Torrens-Spence, M.P.; Liu, P.; Ding, H.; Harich, K.; Gillaspy, G.; Li, J.
Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases
J. Biol. Chem.
288
2376-2387
2013
Petroselinum crispum (Q06086), Arabidopsis thaliana (Q8RY79), Thalictrum flavum subsp. glaucum (Q9AXN7)
Manually annotated by BRENDA team