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, 25C, 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, 25C, TyrAAT1
37.3
L-arogenate
Arabidopsis thaliana
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pH 7.5, 25C, 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
28-30C: optimum, 42C: 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
-
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 4C than when maintained frozen at -20C or at -70C
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