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Information on EC 1.3.1.43 - arogenate dehydrogenase for references in articles please use BRENDA:EC1.3.1.43Word Map on EC 1.3.1.43
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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L-arogenate + NAD+ = L-tyrosine + NADH + CO2
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding motif
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism; TyrA dehydrogenase superfamily
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L-arogenate + NAD+ = L-tyrosine + NADH + CO2
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oxidative decarboxylation
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L-tyrosine biosynthesis III
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Novobiocin biosynthesis
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Biosynthesis of secondary metabolites
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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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arogenic dehydrogenase
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cyclohexadienyl dehydrogenase
dehydrogenase, pretyrosine
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pretyrosine dehydrogenase
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arogenate dehydrogenase
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-
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arogenate dehydrogenase
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cyclohexadienyl dehydrogenase
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cyclohexadienyl dehydrogenase
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cyclohexadienyl dehydrogenase
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cyclohexadienyl dehydrogenase
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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-
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brenda
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brenda
ATCC 27630 and isolated HGH 154
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brenda
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brenda
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brenda
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brenda
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brenda
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-
brenda
-
-
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brenda
JM300
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brenda
JM300
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brenda
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-
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brenda
-
-
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brenda
-
-
-
brenda
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brenda
29108
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brenda
29108
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brenda
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brenda
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brenda
corn
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brenda
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malfunction
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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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L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
L-arogenate + NAD+
L-tyrosine + NADH + CO2
prephenate + NAD+
?
-
-
-
-
?
additional information
?
-
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
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(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
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(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
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i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
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?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
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-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
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-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + 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
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-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
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-
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?
prephenate + NAD(P)+
?
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?
prephenate + NAD(P)+
?
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not prephenate
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prephenate + NAD(P)+
?
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?
prephenate + NAD(P)+
?
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?
prephenate + NAD(P)+
?
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?
prephenate + NAD(P)+
?
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?
additional information
?
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highly specific for arogenate
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additional information
?
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highly specific for arogenate
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additional information
?
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activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
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additional information
?
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activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
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additional information
?
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activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
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additional information
?
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prephenate and L-arogenate dehydrogenase activity on one single protein, termed cyclohexadienyl dehydrogenase
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L-arogenate + NAD+
L-tyrosine + NADH + CO2
prephenate + NAD+
?
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-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + 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
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + 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
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
?
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NAD+
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NAD+
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only weak activity with NADP+, 0.25% of activity with NAD+
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3,4-dihydroxyphenylalanine
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slight inhibition
4-amino-L-phenylalanine
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4-hydroxyphenylacetate
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DL-4-hydroxyphenyllactate
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additional information
-
no inhibition with phenyllactate and benzoate
-
4-hydroxyphenylpyruvate
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4-hydroxyphenylpyruvate
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L-phenylalanine
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slight inhibition
L-phenylalanine
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growth inhibition
L-tyrosine
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no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
no inhibition
L-tyrosine
-
competitive inhibition
L-tyrosine
-
no inhibition
phenylpyruvate
-
-
phenylpyruvate
-
no inhibition
prephenate
-
no inhibition
prephenate
-
no inhibition
prephenate
-
competitive inhibition
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L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
L-tyrosine
-
slightly enhancing the activity
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0.09
L-arogenate
-
-
0.01
NAD+
-
-
0.07
prephenate
-
-
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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
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3.1
-
purified enzyme, substrate prephenate
8.825
-
purified enzyme, substrate L-arogenate
0.4
-
-
additional information
-
-
additional information
-
-
additional information
-
-
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9.5
-
-
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-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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P73906
Synechocystis sp. (strain PCC 6803 / Kazusa);
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25500
-
6 * 25500, SDS-PAGE
28100
-
2 * 28100, SDS-PAGE
32000
-
? * 32000, sequence determination and SDS-PAGE
33000
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
36000
-
2 * 36000, SDS-PAGE
37700
-
2 * 37700, SDS-PAGE
38400
-
2 * 38400, SDS-PAGE
66000
-
dimer, gel filtration
69000
-
gel electrophoresis after cross-linking with dimethylsuberimidate
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?
-
? * 32000, sequence determination and SDS-PAGE
hexamer
-
6 * 25500, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE
dimer
-
2 * 37700, SDS-PAGE
dimer
-
2 * 38400, SDS-PAGE
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
-
dimer
-
2 * 28100, SDS-PAGE
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4
-
7 days, 90% loss of activity
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unstable in absence of glycerol
-
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recombinant from Escherichia coli
-
recombinant His-tagged protein from Escherichia coli
-
-
-
partial
-
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expressed in Escherichia coli
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tyrAc gene, sequence analysis, overexpression of His-tagged protein in Escherichia coli
-
tyrc gene, sequence analysis, expression in Escherichia coli
-
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additional information
-
spontaneous mutant tyrB2 without any activity
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
-
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Berry, A.; Jensen, R.A.; Hendry, A.T.
Enzymic arrangement and allosteric regulation of the aromatic amino acid pathway in Neisseria gonorrhoeae
Arch. Microbiol.
149
87-94
1987
Neisseria gonorrhoeae
brenda
Hund, H.K.; Keller, B.; Lingens, F.
Phenylalanine and tyrosine biosynthesis in sporeforming members of the order Actinomycetales
Z. Naturforsch. C
42
387-393
1987
Actinomadura citrea, Actinoplanes auranticolor, Actinoplanes campanulatus, Actinoplanes missouriensis, Actinoplanes philippinensis, Dactylosporangium thailandense, Micromonospora echinospora, Pilimelia terevasa, Planobispora longispora, Planomonospora venezuelensis, Spirillospora albida, Streptomyces humiferus, Streptosporangium roseum
-
brenda
Ahmad, S.; Jensen, R.A.
Evolution of the biochemical pathway for aromatic amino acid biosynthesis in Serpens flexibilis in relationship to its phylogenetic position
Arch. Microbiol.
147
8-12
1987
Pseudomonas flexibilis
-
brenda
Lingens, F.; Keller, E.; Keller, B.
Arogenate dehydrogenase from Phenylobacterium immobile
Methods Enzymol.
142
513-518
1987
Phenylobacterium immobile
-
brenda
Keller, B.; Keller, E.; Lingens, F.
Arogenate dehydrogenase from Streptomyces phaeochromogenes. Purification and properties
Biol. Chem. Hoppe-Seyler
366
1063-1066
1985
Streptomyces phaeochromogenes
brenda
Mayer, E.; Waldner-Sander, S.; Keller, B.; Keller, E.; Lingens, F.
Purification of arogenate dehydrogenase from Phenylobacterium immobile
FEBS Lett.
179
208-212
1985
Phenylobacterium immobile
brenda
Hund, H.K.; B. r, G.; Lingens, F.
Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis
Z. Naturforsch. C
44
797-801
1989
Actinoplanes missouriensis
brenda
Byng, G.; Whitaker, R.; Flick, C.; Jensen, R.A.
Enzymology of L-tyrosine biosynthesis in corn (Zea mays)
Phytochemistry
20
1289-1292
1981
Zea mays
-
brenda
Hall, G.C.; Jensen, R.A.
Enzymological basis for growth inhibition by L-phenylalanine in the cyanobacterium Synechocystis sp. 29108
J. Bacteriol.
144
1034-1042
1980
Synechocystis sp. 29108, Synechocystis sp.
brenda
Fazel, A.M.; Bowen, J.R.; Jensen, R.A.
Arogenate (pretyrosine) is an obligatory intermediate of L-tyrosine biosynthesis: confirmation in a microbial mutant
Proc. Natl. Acad. Sci. USA
77
1270-1273
1980
Brevibacterium flavum
brenda
Xie, G.; Bonner, C.A.; Jensen, R.A.
Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family
Comp. Biochem. Physiol. C
125
65-83
2000
Pseudomonas stutzeri, Pseudomonas stutzeri JM300
brenda
Xia, T.; Jensen, R.A.
A single cyclohexadienyl dehydrogenase specifies the prephenate dehydrogenase and arogenate dehydrogenase components of the dual pathways to L-tyrosine in Pseudomonas aeruginosa
J. Biol. Chem.
265
20033-20036
1990
Pseudomonas aeruginosa
brenda
Zhao, G.; Xia, T.; Ingram, L.O.; Jensen, R.A.
An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis
Eur. J. Biochem.
212
157-165
1993
Zymomonas mobilis
brenda
Holding, D.; Meeley, R.; Hazebroek, J.; Selinger, D.; Gruis, F.; Jung, R.; Larkins, B.
Identification and characterization of the maize arogenate dehydrogenase gene family
J. Exp. Bot.
61
3663-3673
2010
Zea mays
brenda
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