Information on EC 1.3.1.78 - arogenate dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.1.78
-
RECOMMENDED NAME
GeneOntology No.
arogenate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NADP+ = L-tyrosine + NADPH + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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L-tyrosine biosynthesis II
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Metabolic pathways
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Phenylalanine, tyrosine and tryptophan biosynthesis
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
64295-75-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 23055 and ATCC 14987
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-
Manually annotated by BRENDA team
ATCC 15309
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-
Manually annotated by BRENDA team
strain C1W
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-
Manually annotated by BRENDA team
strain C1W
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-
Manually annotated by BRENDA team
ATCC 29151
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
ATCC 29539
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-
Manually annotated by BRENDA team
CBS3
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-
Manually annotated by BRENDA team
CBS3
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-
Manually annotated by BRENDA team
NADP-dependent prephenate and pretyrosine dehydrogenase copurified, multifunctional protein ?
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-
Manually annotated by BRENDA team
corn
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Manually annotated by BRENDA team
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 + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
show the reaction diagram
prephenate + NAD(P)+
?
show the reaction diagram
prephenate + NADP+
3-(4-hydroxyphenyl)-2-oxopropanoate + CO2 + NADPH
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cis-aconitate
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L-phenylalanine
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slight inhibition
L-tyrosine
m-Fluoro-DL-tyrosine
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N-Acetyl-DL-tyrosine
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p-hydroxymercuribenzoate
prephenate
additional information
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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 hide
LITERATURE
IMAGE
0.0526
arogenate
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pH 7.5, 25°C, TyrAAT1
0.0001 - 0.34
L-arogenate
0.005 - 0.075
NADP+
17
prephenate
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
84.2
arogenate
Arabidopsis thaliana
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pH 7.5, 25°C, TyrAAT1
37.3
L-arogenate
Arabidopsis thaliana
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pH 7.5, 25°C, TyrAAT2
3.4
prephenate
Arabidopsis thaliana
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.8 - 115
AMP
5.8 - 42.9
cis-aconitate
0.078 - 0.089
L-Tyr
0.0075 - 0.06
L-tyrosine
0.0539 - 0.0588
NADPH
2.4 - 22.5
prephenate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0024
0.0039
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ATCC 23055
0.0043
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ATCC 14987
0.0078
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0.0109
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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enzyme activity dropps below pH 6.5 and above pH 8.5
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the two Arabidopsis arogenate dehydrogenase proteins and the six arogenate dehydratase proteins are all targeted within the plastid
Manually annotated by BRENDA team
additional information
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no detection in the cytosol
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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2 * 32000, SDS-PAGE
52000
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gel filtration
66000
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1 * 66000, recombinant TyrAAT1, SDS-PAGE
67000
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recombinant TyrAAT1, gel filtration
68000
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gel filtration
70000
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gel filtration
158000
210000
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ATCC 23055, gel filtration
600000
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above, recombinant TyrAAT2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 66000, recombinant TyrAAT1, SDS-PAGE
oligomer
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recombinant TyrAAT2
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
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
ATCC 23055, partial
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partial
partial, NADP-dependent prephenate and pretyrosine dehydrogenase copurified, probably multifunctional protein
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recombinant enzyme expressed in Escherichia coli
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TyrAAT1; TyrAAT2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
tyrA gene, overexpression in Escherichia coli, 3 different plasmids TyrA-ATcM36, TyrA-ATlM36, TyrA-AT2
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TyrAAT1 overproduced in Escherichia coli; TyrAAT2 overproduced in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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mutant pheA5 and double-mutant pheA5 shkA1 by mutagenesis and growth selection, reduced activity