Information on EC 1.3.1.43 - arogenate dehydrogenase

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

EC NUMBER
COMMENTARY
1.3.1.43
-
RECOMMENDED NAME
GeneOntology No.
arogenate dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
show the reaction diagram
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
show the reaction diagram
substrate binding motif
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
show the reaction diagram
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
Pseudomonas stutzeri JM300
-
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tyrosine biosynthesis III
-
-
tyrosine metabolism
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Novobiocin biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arogenate:NAD+ oxidoreductase (decarboxylating)
See also EC 1.3.1.12 (prephenate dehydrogenase), EC 1.3.1.78 [arogenate dehydrogenase (NADP+)] and EC 1.3.1.79 (arogenate dehydrogenase [NAD(P)+]).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ADH
-
-
-
-
arogenate dehydrogenase
-
-
-
-
arogenate dehydrogenase
-
-
arogenic dehydrogenase
-
-
-
-
cyclohexadienyl dehydrogenase
-
-
cyclohexadienyl dehydrogenase
-
-
cyclohexadienyl dehydrogenase
Pseudomonas stutzeri JM300
-
-
-
cyclohexadienyl dehydrogenase
-
-
dehydrogenase, pretyrosine
-
-
-
-
pretyrosine dehydrogenase
-
-
-
-
zmAroDH-1
-
-
zmAroDH-2
-
-
zmAroDH-3
-
-
CAS REGISTRY NUMBER
COMMENTARY
64295-75-6
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
Synechocystis sp. 29108
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
Pseudomonas stutzeri JM300
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Synechocystis sp. 29108
-
-
-
?
prephenate + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
prephenate + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
prephenate + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
prephenate + NAD(P)+
?
show the reaction diagram
-
-
-
-
?
prephenate + NAD(P)+
?
show the reaction diagram
-
not prephenate
-
-
-
prephenate + NAD(P)+
?
show the reaction diagram
Pseudomonas stutzeri JM300
-
-
-
-
?
prephenate + NAD+
?
show the reaction diagram
-
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
Pseudomonas stutzeri JM300
-
-
-
?
additional information
?
-
-
highly specific for arogenate
-
-
-
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
-
-
-
additional information
?
-
Pseudomonas stutzeri JM300
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Synechocystis sp. 29108
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
Pseudomonas stutzeri JM300
-
-
-
?
prephenate + NAD+
?
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-dihydroxyphenylalanine
-
slight inhibition
4-amino-L-phenylalanine
-
-
4-hydroxybenzoate
-
-
4-hydroxyphenylacetate
-
-
4-hydroxyphenylpyruvate
-
-
4-hydroxyphenylpyruvate
-
-
D-tyrosine
-
-
DL-4-hydroxyphenyllactate
-
-
L-phenylalanine
-
growth inhibition
L-phenylalanine
-
slight inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
no inhibition
phenylpyruvate
-
-
phenylpyruvate
-
no inhibition
prephenate
-
no inhibition
prephenate
-
competitive inhibition
prephenate
-
no inhibition
m-Fluoro-DL-tyrosine
-
-
additional information
-
no inhibition with phenyllactate and benzoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
L-arogenate
-
-
0.15
L-arogenate
-
-
0.17
L-arogenate
-
-
0.18
L-arogenate
-
-
0.3
L-arogenate
-
-
0.56
L-arogenate
-
-
0.66
L-arogenate
-
-
0.91
L-arogenate
-
-
0.057
NAD+
-
-
0.09
NAD+
-
-
0.41
NAD+
-
-
0.07
prephenate
-
-
0.07
prephenate
-
-
0.25
prephenate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
4-hydroxylphenylpyruvate
-
-
0.016
L-tyrosine
-
competitive inhibition
0.05
L-tyrosine
-
with L-arogenate as variable substrate, competitive inhibition
0.06
L-tyrosine
-
with prephenate as variable substrate, competitive inhibition
0.26
L-tyrosine
-
competitive inhibition
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0017
-
ATCC 27360
0.0058
-
HGH 154
3.1
-
purified enzyme, substrate prephenate
8.825
-
purified enzyme, substrate L-arogenate
18.8
-
purified enzyme
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61700
-
gel filtration
390782
66000
-
dimer, gel filtration
390802
66300
-
gel filtration
390783
68000
-
gel filtration
390785
69000
-
gel electrophoresis after cross-linking with dimethylsuberimidate
390784
150000
-
gel filtration
390803
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
? * 32000, sequence determination and SDS-PAGE
dimer
-
2 * 37700, SDS-PAGE
dimer
-
2 * 28100, SDS-PAGE
dimer
-
2 * 38400, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
dimer
Pseudomonas stutzeri JM300
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
-
hexamer
-
6 * 25500, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
7 days, 90% loss of activity
390785
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in absence of glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tyrAc gene, sequence analysis, overexpression of His-tagged protein in Escherichia coli
-
expressed in Escherichia coli
-
tyrc gene, sequence analysis, expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
spontaneous mutant tyrB2 without any activity
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
additional information
Synechocystis sp. 29108
-
spontaneous mutant Phe r19, growth selection, reduced activity
-