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Enzyme Nomenclature
Information on EC 1.3.1.43 - arogenate dehydrogenase
for references in articles please use BRENDA:EC1.3.1.43
Word Map on EC 1.3.1.43
- 1.3.1.43
- prephenate
- l-tyrosine
-
dehydratase
- chorismate
-
mutase
- l-phenylalanine
- 4-hydroxyphenylpyruvate
- shikimate
- phenylpyruvate
-
3-deoxy-d-arabino-heptulosonate
-
7-phosphate
- mobilis
- dahp
- zymomonas
- l-tyr
-
t-proteins
-
mutase-prephenate
-
5-enolpyruvylshikimate
- herbicola
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.3.1.43
-
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RECOMMENDED NAME
GeneOntology No.
arogenate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
-
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-arogenate:NAD+ 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). NAD+-specific enzymes have been reported from some bacteria [2] and plants [3]. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
64295-75-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
a maize opaque endosperm mutant (mto140), which shows retarded vegetative growth, is described. The opaque phenotype co-segregates with a mutator transposon insertion in an arogenate dehydrogenase gene (zmAroDH-1). Mto140/arodh-1 seeds show a general reduction in zein storage protein accumulation and an elevated lysine phenotype typical of other opaque endosperm mutants; a mutator insertion at an equivalent position in AroDH-3, the most closely related family member to AroDH-1, is associated with opaque endosperm and stunted vegetative growth phenotypes
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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
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
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
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
-
-
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
-
-
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
-
-
additional information
?
-
-
prephenate and L-arogenate dehydrogenase activity on one single protein, termed cyclohexadienyl dehydrogenase
-
-
-
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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
-
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
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition with phenyllactate and benzoate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
L-tyrosine
-
with L-arogenate as variable substrate, competitive inhibition
0.06
L-tyrosine
-
with prephenate as variable substrate, competitive inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
69000
-
gel electrophoresis after cross-linking with dimethylsuberimidate
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
dimer
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tyrAc gene, sequence analysis, overexpression of His-tagged protein in Escherichia coli
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.43)
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