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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 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.78 arogenate dehydrogenase (NADP+)
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].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.3.1.78
-
kinase-inactive
- prephenate
-
gadd45
-
malformation
-
annexin
-
ifngamma
-
neurulation
-
perinuclear
-
calcium-dependent
-
mekks
showSynonyms
tyra1, tyra2, tyraat1, tyrasy, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TyrAa
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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 SOURCE
PATHWAYS
MetaCyc
L-tyrosine biosynthesis II
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prephenate + NADP+
3-(4-hydroxyphenyl)-2-oxopropanoate + CO2 + NADPH
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: exclusive metabolic route to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: important enzyme in regulation of tyrosine biosynthesis
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: rapid equilibrium random mechanism in which two dead-end complexes, enzyme-NADPH-arogenate and enzyme-NADP+-tyrosine are formed
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
Substrates: -
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: specific for, no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prephenate and NAD+
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: exclusive metabolic route to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: important enzyme in regulation of tyrosine biosynthesis
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
Substrates: -
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
L-arogenate + NADP+
L-tyrosine + NADPH + CO2
-
Substrates: enzyme of the arogenate pathway
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NADP-dependent prephenate and pretyrosine dehydrogenase copurified, multifunctional protein ?
-
-
brenda
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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
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
malfunction
metabolism
malfunction
TyrA2 knockout leads to slow growth with reticulate leaves. TyrA2 deficiency alters the levels of multiple amino acids but not of tyrosine
malfunction
TyrA1 suppression reduces seed yield due to impaired anther dehiscence
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
metabolism
most plants synthesize tyrosine by TyrA arogenate dehydrogenases. TyrA1 and TyrA2 have distinct and overlapping functions in flower and leaf development, respectively. The imbalance of tyrosine, caused by altered TyrA activity and regulation, impacts growth and development of Arabidopsis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). P73906_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
279
0
30216
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
158000
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SUBUNIT
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutant pheA5 and double-mutant pheA5 shkA1 by mutagenesis and growth selection, reduced activity
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fazel, A.M.; Jensen, R.A.
Obligatory biosynthesis of L-tyrosine via the pretyrosine branchlet in coryneform bacteria
J. Bacteriol.
138
805-815
1979
Corynebacterium ammoniagenes, Corynebacterium glutamicum, [Brevibacterium] flavum
brenda
Rubin, J.L.; Jensen, R.A.
Enzymology of L-tyrosine biosynthesis in mung bean (Vigna radiata [L.] Wilczek)
Plant Physiol.
64
727-734
1979
Vigna radiata
brenda
Byng, G.S.; Berry, A.; Jensen, R.A.
Evolutionary implications of features of aromatic amino acid biosynthesis in the genus Acinetobacter
Arch. Microbiol.
143
122-129
1985
Acinetobacter calcoaceticus, Acinetobacter lwoffii, Acinetobacter sp., Acinetobacter sp. C1W
brenda
Bonner, C.; Jensen, R.
Arogenate dehydrogenase
Methods Enzymol.
142
488-494
1987
Corynebacterium glutamicum, Euglena gracilis, Nicotiana sylvestris, Phenylobacterium immobile, Sorghum bicolor, Streptomyces phaeochromogenes, Vigna radiata, Zea mays, [Brevibacterium] flavum
brenda
Connelly, J.A.; Conn, E.E.
Tyrosine biosynthesis in Sorghum bicolor: isolation and regulatory properties of arogenate dehydrogenase
Z. Naturforsch. C
41
69-78
1986
Sorghum bicolor
brenda
Keller, B.; Keller, E.; Klages, U.; Lingens, F.
Aromatic amino acid biosynthesis in a 4-chlorobenzoic acid degrading Pseudomonas species; phenylalanine and tyrosine synthesis via arogenate
Syst. Appl. Microbiol.
4
27-33
1983
Pseudomonas sp., Pseudomonas sp. CBS3
brenda
Gaines, C.G.; Byng, G.S.; Whitaker, R.J.; Jensen, R.A.
L-tyrosine regulation and biosynthesis via arogenate dehydrogenase in suspension-cultured cells of Nicotiana silvestris Speg. et Comes
Planta
156
233-240
1982
Nicotiana sylvestris
brenda
Keller, B.; Keller, E.; Sussmuth, R.; Lingens, F.
Arogenate (pretyrosine) as an obligatory precursor of L-tyrosine biosynthesis in Flavobacterium devorans
FEMS Microbiol. Lett.
13
3-4
1982
Sphingomonas paucimobilis
-
brenda
Rippert, P.; Matringe, M.
Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains
Plant Mol. Biol.
48
361-368
2002
Arabidopsis thaliana
brenda
Bonner, C.A.; Fischer, R.S.; Schmidt, R.R.; Miller, P.W.; Jensen, R.A.
Distinctive enzymes of aromatic amino acid biosynthesis that are highly conserved in land plants are also present in the chlorophyte alga Chlorella sorokiniana
Plant Cell Physiol.
36
1013-1022
1995
Chlorella sorokiniana, Nicotiana sylvestris
-
brenda
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
brenda
Rippert, P.; Matringe, M.
Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana
Eur. J. Biochem.
269
4753-4761
2002
Arabidopsis thaliana
brenda
Legrand, P.; Dumas, R.; Seux, M.; Rippert, P.; Ravelli, R.; Ferrer, J.L.; Matringe, M.
Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction
Structure
14
767-776
2006
Synechocystis sp.
brenda
Rippert, P.; Puyaubert, J.; Grisollet, D.; Derrier, L.; Matringe, M.
Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis
Plant Physiol.
149
1251-1260
2009
Arabidopsis thaliana
brenda
Schenck, C.A.; Chen, S.; Siehl, D.L.; Maeda, H.A.
Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes
Nat. Chem. Biol.
11
52-57
2015
Arabidopsis thaliana (Q944B6), Arabidopsis thaliana (Q9LMR3)
brenda
de Oliveira, M.V.V.; Jin, X.; Chen, X.; Griffith, D.; Batchu, S.; Maeda, H.A.
Imbalance of tyrosine by modulating TyrA arogenate dehydrogenases impacts growth and development of Arabidopsis thaliana
Plant J.
97
901-922
2019
Arabidopsis thaliana (Q944B6), Arabidopsis thaliana (Q9LMR3), Arabidopsis thaliana
brenda
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