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Information on EC 1.3.1.78 - arogenate dehydrogenase (NADP+)
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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].
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Word Map
- 1.3.1.78
-
kinase-inactive
- prephenate
-
gadd45
-
malformation
-
annexin
-
ifngamma
-
neurulation
-
perinuclear
-
calcium-dependent
-
mekks
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ADH1, ADH2, arogenate dehydrogenase, arogenate dehydrogenase isoform 1, arogenate dehydrogenase isoform 2, cyclohexadienyl dehydrogenase, TyrAa, TyrAAT, 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
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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
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
-
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
-
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 + 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
-
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
-
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
-
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
-
-
?
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 SUBSTRATE
NATURAL 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
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
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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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
115
AMP
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ 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
25.9
AMP
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
17.8
AMP
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
42.9
cis-aconitate
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
27.7
cis-aconitate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1
25.3
cis-aconitate
-
pH 7.5, 25°C, with 0.2 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
5.8
cis-aconitate
-
pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
0.0075
L-tyrosine
-
pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2
0.0166
L-tyrosine
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2
0.0142
L-tyrosine
-
pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1
0.0081
L-tyrosine
-
pH 7.5, 25°C, with 0.05 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
0.0539
NADPH
-
pH 7.5, 25°C, with 0.02 mM NADP+ as fixed substrate and arogenate 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
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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
metabolism
in plants, L-Tyr is syntheÂsized 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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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). TYRA1_ARATH
640
0
72301
Swiss-Prot
Chloroplast (Reliability: 3)
TYRA2_ARATH
358
0
40633
Swiss-Prot
Chloroplast (Reliability: 4)
Q31QH7_SYNE7
Synechococcus elongatus (strain PCC 7942 / FACHB-805)
323
0
34660
TrEMBL
-
K4C5K7_SOLLC
272
0
31052
TrEMBL
Mitochondrion (Reliability: 5)
K8GTM0_9CYAN
281
0
30424
TrEMBL
-
A0A2I0BGJ1_9ASPA
163
0
18124
TrEMBL
Mitochondrion (Reliability: 5)
A0A2H9ZV99_9ASPA
416
0
46869
TrEMBL
Chloroplast (Reliability: 1)
A0A2G9G7M3_9LAMI
210
0
23681
TrEMBL
other Location (Reliability: 5)
A0A7Y0NWN4_9CYAN
277
0
30255
TrEMBL
-
Q46IQ2_PROMT
Prochlorococcus marinus (strain NATL2A)
291
0
31927
TrEMBL
-
A0A2P6RIL4_ROSCH
684
0
77056
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6RU98_ROSCH
601
0
67884
TrEMBL
Secretory Pathway (Reliability: 5)
A0A1Z5JNH2_FISSO
425
0
47605
TrEMBL
Secretory Pathway (Reliability: 4)
E0RS32_SPITD
Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1)
273
0
30801
TrEMBL
-
Q3M4U1_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
284
0
30640
TrEMBL
-
A0A2P6RU96_ROSCH
118
0
13446
TrEMBL
other Location (Reliability: 2)
A0A2P6RVV1_ROSCH
384
0
43781
TrEMBL
Mitochondrion (Reliability: 5)
F8F0F0_TRECH
Treponema caldarium (strain ATCC 51460 / DSM 7334 / H1)
263
0
29781
TrEMBL
-
A0A1Z5J658_FISSO
425
0
47560
TrEMBL
Secretory Pathway (Reliability: 4)
K9TUB8_CHRTP
Chroococcidiopsis thermalis (strain PCC 7203)
280
0
30007
TrEMBL
-
G7K798_MEDTR
104
0
11765
TrEMBL
Secretory Pathway (Reliability: 5)
I1K197_SOYBN
685
0
77745
TrEMBL
Chloroplast (Reliability: 5)
A0A2G9HRZ4_9LAMI
253
0
28749
TrEMBL
other Location (Reliability: 3)
A0A1J0AC61_9CYAN
288
0
31062
TrEMBL
-
G7J2E9_MEDTR
268
0
30035
TrEMBL
other Location (Reliability: 5)
K7MLB3_SOYBN
690
0
78320
TrEMBL
Chloroplast (Reliability: 4)
I1M7P5_SOYBN
266
0
30041
TrEMBL
other Location (Reliability: 4)
A0A2P6RUA1_ROSCH
469
0
53222
TrEMBL
Secretory Pathway (Reliability: 5)
A0A072UR36_MEDTR
679
0
76770
TrEMBL
Chloroplast (Reliability: 5)
K9Z1U0_CYAAP
Cyanobacterium aponinum (strain PCC 10605)
278
0
30241
TrEMBL
-
Q318H7_PROM9
Prochlorococcus marinus (strain MIT 9312)
279
0
30460
TrEMBL
-
A0A0D2NPT4_9CHLO
368
0
40901
TrEMBL
Mitochondrion (Reliability: 3)
Q111D4_TRIEI
Trichodesmium erythraeum (strain IMS101)
283
0
31229
TrEMBL
-
K9ZLR8_ANACC
Anabaena cylindrica (strain ATCC 27899 / PCC 7122)
279
0
30239
TrEMBL
-
A0A2K5B250_MUCPR
266
0
30370
TrEMBL
other Location (Reliability: 4)
A0A0L0LC32_9BACT
246
0
27738
TrEMBL
-
A0A2I0B0M7_9ASPA
320
0
35786
TrEMBL
Chloroplast (Reliability: 4)
K9YK15_CYASC
Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202)
279
0
30531
TrEMBL
-
G7K796_MEDTR
266
0
30140
TrEMBL
other Location (Reliability: 4)
F0RTR9_SPHGB
Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
252
0
28154
TrEMBL
-
K9RT11_SYNP3
Synechococcus sp. (strain ATCC 27167 / PCC 6312)
278
0
29810
TrEMBL
-
P73906_SYNY3
Synechocystis sp. (strain 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
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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.
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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)
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