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Information on EC 1.3.1.78 - arogenate dehydrogenase (NADP+)

for references in articles please use BRENDA:EC1.3.1.78
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EC Tree
IUBMB Comments
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly [2,3].
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This record set is specific for:
UNIPROT: P73906
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Word Map
  • 1.3.1.78
  • kinase-inactive
  • prephenate
  • gadd45
  • malformation
  • annexin
  • ifngamma
  • neurulation
  • perinuclear
  • calcium-dependent
  • mekks
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
tyra1, tyra2, tyraat1, tyrasy, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
show the reaction diagram
mechanism is probably steady-state random order
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arogenate:NADP+ oxidoreductase (decarboxylating)
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NADP+-dependent enzymes usually predominate in higher plants.The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 and the TyrAAT1 isoform of the plant Arabidopsis thaliana cannot use prephenate as a substrate, while the Arabidopsis isoform TyrAAT2 can use it very poorly [2,3].
CAS REGISTRY NUMBER
COMMENTARY hide
64295-75-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
show the reaction diagram
additional information
?
-
no activity with prephenate and NAD+
-
-
?
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-arogenate + NADP+
L-tyrosine + NADPH + CO2
show the reaction diagram
enzyme of the arogenate pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
no activity with NAD+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.331
L-arogenate
pH 8.6, 25°C
0.038
NADP+
pH 8.6, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.078 - 0.089
L-Tyr
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 42
28-30°C: optimum, 42°C: 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
P73906_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
279
0
30216
TrEMBL
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
full activity is retained in repeated freeze-thaw cycles, when concentrations of 0.01 mg of protein per ml or more are maintained
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is less stable during storage at 4°C than when maintained frozen at -20°C or at -70°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bonner, C.A.; Jensen, R.A.; Gander, J.E.; Keyhani, N.O.
A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis
Biochem. J.
382
279-291
2004
Anabaena sp., Chlorella sorokiniana, Fischerella sp., Porphyridium purpureum, Prochlorothrix hollandica, Synechococcus elongatus PCC 6301, Synechocystis sp., Synechocystis sp. PCC 6803 (P73906), Synechocystis sp. PCC 6902
Manually annotated by BRENDA team