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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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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs; prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs
metabolism
in plants, L-Tyr is synthesized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH; in plants, L-Tyr is synthesized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH
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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
gene ADH1, phylogenetic analysis; gene ADH2, phylogenetic analysis
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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