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Information on EC 4.1.1.25 - tyrosine decarboxylase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q60358

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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:
Methanocaldococcus jannaschii
UNIPROT: Q60358
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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, dtdc2, tyrosine/dopa decarboxylase, vwtydc, tyr decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Decarboxylase, tyrosine
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-
-
-
ELI5
-
-
-
-
L-(-)-Tyrosine apodecarboxylase
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-
-
-
L-Tyrosine decarboxylase
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-
-
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TDC
-
-
-
-
TYDC/DODC
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-
-
-
Tyrosine/Dopa decarboxylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
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-aspartate
3-aminopropionic acid + CO2
show the reaction diagram
95% of the activity with L-tyrosine
-
-
?
L-glutamate
4-aminobutyric acid + CO2
show the reaction diagram
80% of the activity with L-tyrosine
-
-
?
L-Tyrosine
Tyramine + CO2
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroxylamine
2 mM, complete inhibition
O-Methylhydroxylamine
2 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
2 * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 45000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
10 min, enzyme retains full activity
110
10 min, 68% loss of activity
121
10 min, complete loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transformed into Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kezmarsky, N.D.; Xu, H.; Graham, D.E.; White, R.H.
Identification and characterization of a L-tyrosine decarboxylase in Methanocaldococcus jannaschii
Biochim. Biophys. Acta
1722
175-182
2005
Methanocaldococcus jannaschii (Q60358), Methanocaldococcus jannaschii
Manually annotated by BRENDA team