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Information on EC 4.1.1.25 - tyrosine decarboxylase and Organism(s) Papaver somniferum and UniProt Accession P54768

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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:
Papaver somniferum
UNIPROT: P54768
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Word Map
The taxonomic range for the selected organisms is: Papaver somniferum
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Reaction Schemes
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
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tyrosine/Dopa decarboxylase-1
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tyrosine/Dopa decarboxylase-2
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Decarboxylase, tyrosine
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-
-
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ELI5
-
-
-
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L-(-)-Tyrosine apodecarboxylase
-
-
-
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L-Tyrosine decarboxylase
-
-
-
-
TDC
-
-
-
-
TYDC/DODC
-
-
-
-
tyrosine decarboxylase
-
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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
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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-Tyrosine
Tyramine + CO2
show the reaction diagram
-
-
?
L-3,4-Dihydroxyphenylalanine
Dopamine + CO2
show the reaction diagram
-
-
-
-
?
L-Dopa
dopamine + CO2
show the reaction diagram
-
-
-
?
L-Tyr
?
show the reaction diagram
-
catalyzes an early step in the biosynthesis of isoquinoline alkaloids
-
-
?
L-Tyr
Tyramine + CO2
show the reaction diagram
-
-
-
?
L-Tyrosine
Tyramine + CO2
show the reaction diagram
additional information
?
-
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
-
-
?
L-Tyr
?
show the reaction diagram
-
catalyzes an early step in the biosynthesis of isoquinoline alkaloids
-
-
?
L-Tyrosine
Tyramine + CO2
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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PLP, binding structure, overview. The cofactor is covalently attached to the epsilon-amino group of K321 to form an internal aldimine via a Schiff-base interaction. The protonated pyridine nitrogen of PLP forms a pair of salt bridges to the carboxyl group of D289. The PLP pyridine ring is anchored by the methyl group of A291 and the imidazole ring of H205. The O3 atom of the pyridine ring of PLP seems to interact with T264 adjacent water molecules. The phosphate moiety of PLP is stabilized by a number of interactions with T169, C170, N318 of one subunit, and R373 of the other subunit
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
opium poppy
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
recombinant TyDC5, vascular cylinder surrounding the xylem
Manually annotated by BRENDA team
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recombinant TyDC5, xylem parenchyma
Manually annotated by BRENDA team
additional information
-
recombinant TyDC5 expression pattern, not in poppy laticifers, about 15 members of the TyDC gene family show differences in developmental, tissue-specific and inducible gene expression
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYDC1_PAPSO
518
0
57020
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 25 mM HEPES, pH 7.0, and 0.04 mM pyridoxal 5'-phosphate, with 0.001 ml of reservoir solution containing 0.2 M NaOAc and 1 M NH4H2PO4, and equilibration against 0.45 ml of reservoir solution, X-ray diffraction structure determination and analysis at 3.1 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged enzyme by affinity and anion exchange chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of TyDC5 fused to beta-glucuronidase in Papaver somniferum and in Nicotiana tabacum
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gene tdc, recombinant expression of tagged enzyme
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transgenic Nicotiana tabacum cv. Xanthi is engineered to constitutively express tobacco THT (EC 2.3.1.110). A T1 plant overexpressing THT is crossbred with T1 tobacco expressing opium poppy TYDC2 (EC 4.1.1.25), to produce a T2 line with elevated THT and TYDC activities compared with wild type plants
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TYDC transgenic lines obtained by transformation of Nicotiana tabacum with agrobacterium tumefaciens containing Papaver somniferum TYC2 cDNA
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TYDC-2, expression in Nicotiana tabacum cv Xanthi, altered biological and physiological phenotype of transgenic tobacco lines
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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.; de Luca, V.
Differential and tissue-specific expression of a gene family for tyrosine/dopa decarboxylase in opium poppy
J. Biol. Chem.
269
26684-26690
1994
Papaver somniferum
Manually annotated by BRENDA team
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
El-Ahmady, S.H.; Nessler, C.L.
Cellular localization of tyrosine decarboxylase expression in transgenic opium poppy and tobacco
Plant Cell Rep.
20
313-317
2001
Papaver somniferum
-
Manually annotated by BRENDA team
Guillet, G.; Poupart, J.; Basurco, J.; De Luca, V.
Expression of tryptophan decarboxylase and tyrosine decarboxylase genes in tobacco results in altered biochemical and physiological phenotypes
Plant Physiol.
122
933-943
2000
Papaver somniferum, Papaver somniferum TYDC-2
Manually annotated by BRENDA team
Hagel, J.M.; Facchini, P.J.
Elevated tyrosine decarboxylase and tyramine hydroxycinnamoyltransferase levels increase wound-induced tyramine-derived hydroxycinnamic acid amide accumulation in transgenic tobacco leaves
Planta
221
904-914
2005
Papaver somniferum
Manually annotated by BRENDA team
Guan, H.; Song, S.; Robinson, H.; Liang, J.; Ding, H.; Li, J.; Han, Q.
Structural basis of the substrate specificity and enzyme catalysis of a Papaver somniferum tyrosine decarboxylase
Front. Mol. Biosci.
4
5-5
2017
Papaver somniferum
Manually annotated by BRENDA team