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Enzyme Nomenclature
Information on EC 1.3.1.78 - arogenate dehydrogenase (NADP+)
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.3.1.78
-
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RECOMMENDED NAME
GeneOntology No.
arogenate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
-
-
-
-
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
mechanism is probably steady-state random order
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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CAS REGISTRY NUMBER
COMMENTARY
64295-75-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NADP-dependent prephenate and pretyrosine dehydrogenase copurified, multifunctional protein ?
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prephenate + NADP+
3-(4-hydroxyphenyl)-2-oxopropanoate + CO2 + NADPH
-
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
exclusive metabolic route to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
important enzyme in regulation of tyrosine biosynthesis
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
rapid equilibrium random mechanism in which two dead-end complexes, enzyme-NADPH-arogenate and enzyme-NADP+-tyrosine are formed
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
specific for, no activity with prephenate and NAD+
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
specific for, no activity with prephenate and NAD+
-
-
?
additional information
?
-
-
TyrAAT1 is four times more efficient in catalyzing arogenate dehydrogenase reaction than TyrAAT2. TyrAAT2 presents a weak prephenate dehydrogenase activity whereas Tyr-AAT1 does not
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-
-
additional information
?
-
-
no activity with prephenate and NAD+
-
-
-
additional information
?
-
-
no activity with prephenate and NAD+
-
-
-
additional information
?
-
-
no activity with prephenate and NAD+
-
-
-
additional information
?
-
-
no activity with prephenate and NAD+
-
-
-
additional information
?
-
no activity with prephenate and NAD+
-
-
-
additional information
?
-
-
no activity with prephenate and NAD+
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
exclusive metabolic route to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
important enzyme in regulation of tyrosine biosynthesis
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
P73906
enzyme of the arogenate pathway
-
-
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
enzyme of the arogenate pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
almost completely insensitive to feedback inhibition by tyrosine. Phenylalanine and tryptophan show no effect at concentrations of up to 1 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.8
AMP
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
25.9
AMP
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
73.9
AMP
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
115
AMP
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
5.8
cis-aconitate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
25.3
cis-aconitate
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
27.7
cis-aconitate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
42.9
cis-aconitate
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
0.0075
L-tyrosine
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
0.0081
L-tyrosine
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
0.0142
L-tyrosine
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
0.0166
L-tyrosine
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
0.0539
NADPH
-
pH 7.5, 25°C, with 0.02 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
0.0588
NADPH
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
2.4
prephenate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
4.2
prephenate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
20.2
prephenate
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
22.5
prephenate
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0024
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
33
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the two Arabidopsis arogenate dehydrogenase proteins and the six arogenate dehydratase proteins are all targeted within the plastid
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
158000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop method, structure of TyrAsy in complex with NADP+ is refined to 1.6 A. The asymmetric unit contains two TyrAsy homodimers, with each monomer consisting of a nucleotide binding N-terminal domain and a particularly unique alpha-helical C-terminal dimerization domain
-
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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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
partial, NADP-dependent prephenate and pretyrosine dehydrogenase copurified, probably multifunctional protein
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tyrA gene, overexpression in Escherichia coli, 3 different plasmids TyrA-ATcM36, TyrA-ATlM36, TyrA-AT2
-
TyrAAT1 overproduced in Escherichia coli; TyrAAT2 overproduced in Escherichia coli
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutant pheA5 and double-mutant pheA5 shkA1 by mutagenesis and growth selection, reduced activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.78)
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