Information on EC 4.2.1.91 - arogenate dehydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.91
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RECOMMENDED NAME
GeneOntology No.
arogenate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate = L-phenylalanine + H2O + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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L-phenylalanine biosynthesis II
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Metabolic pathways
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Phenylalanine, tyrosine and tryptophan biosynthesis
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phenylalanine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-arogenate hydro-lyase (decarboxylating; L-phenylalanine-forming)
Also acts on prephenate and D-prephenyllactate. cf. EC 4.2.1.51, prephenate dehydratase.
CAS REGISTRY NUMBER
COMMENTARY hide
76600-70-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 13184 and ATCC 11568
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Manually annotated by BRENDA team
unicellular chlorophyte alga
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ATCC 25304
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Manually annotated by BRENDA team
no activity in Acinetobacter calcoaceticus
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Manually annotated by BRENDA team
ATCC 33243
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Manually annotated by BRENDA team
ATX2752
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Manually annotated by BRENDA team
ATX2752
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview; plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview; plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview; plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview; plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview; plant ADTs and prephenate dehydratases, EC 4.2.1.51, share many common features allowing them to act as dehydratase/decarboxylases, but group independently conferring distinct substrate specificities, sequence comparisons, overview
malfunction
metabolism
physiological function
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the enzyme is required for biosynthesis of L-phenylalanine. Specific ADTs are differentially regulated so as to control Phe biosynthesis for protein synthesis versus its much more massive deployment for phenylpropanoid metabolism, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arogenate
L-phenylalanine + CO2 + H2O
show the reaction diagram
L-arogenate
L-phenylalanine + H2O + CO2
show the reaction diagram
prephenate
phenylpyruvate + CO2 + H2O
show the reaction diagram
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
prephenyl lactate
phenyllactate + CO2 + H2O
show the reaction diagram
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D-beta-(1-carboxy-4-hydroxy-2,5-cyclohexadiene-1-yl)-lactic acid, isolated from Neurospora crassa
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arogenate
L-phenylalanine + CO2 + H2O
show the reaction diagram
L-arogenate
L-phenylalanine + H2O + CO2
show the reaction diagram
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-2-Thienylalanine
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L-arogenate
L-phenylalanine
p-Fluorophenylalanine
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prephenate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-phenylalanine
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activity stimulated by, reaction rate 105%
D-tyrosine
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activity stimulated by, reaction rate 102%
p-hydroxy-phenylacetonitrile
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activity stimulated by, reaction rate 104%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.17
arogenate
0.0488 - 10.08
L-arogenate
0.17 - 2.44
prephenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.194 - 6.1
L-arogenate
0.012 - 0.16
prephenate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.48 - 18.51
L-arogenate
883
0.03 - 0.08
prephenate
353
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-arogenate
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; pH 7.5, 22C; pH 7.5, 37C
0.024 - 61.5
L-phenylalanine
0.4
prephenate
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; pH 7.5, 22C; pH 7.5, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
L-phenylalanine
Oryza sativa
A8CF65
wild-type, rice ADT is a bifunctional enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0012
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crude extract
0.00425
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0.0063
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ATCC 13184
0.0483
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L-arogenate dehydratase activity
0.158
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prephenate dehydratase activity
23.68
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L-arogenate dehydratase activity
29.4
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prephenate dehydratase activity
102.8
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purified recombinant enzyme, with L-arogenate as substrate
307.7
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purified recombinant enzyme, with prephenate as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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ATCC 13184
7 - 8.5
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ATCC 13184
7.5 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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L-Phe/Tyr and general amino acid pools development during weeks in tissues of isozyme knockout mutants compared to the wild-type enzyme, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
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4 * 18000, SDS-PAGE
28000
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x * 28000, SDS-PAGE
29500
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2 * 29500, SDS-PAGE, gel filtration; 2 * 29500, SDS-PAGE, homodimer; 2 * 30480, calculated, 2 * 29500, SDS-PAGE
30480
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2 * 30480, calculated from amino acis sequence; calculated from cloned gene pheC
43400
sequence analysis
45900
sequence analysis
47300
sequence analysis
73000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 28000, SDS-PAGE
tetramer
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4 * 18000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
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ATCC 13184, activity declines sharply above
648473, 648475
9
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rate declines at pH 9.0 and above
648476
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, overnight dialysis against 100 mM Epps, pH 8.0, 20% ethylene glycol, 0.1 mM EDTA, 2 mM DTT, activity is stable for 6 months
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-80C, enzyme activity in crude extract is stable for at least 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by fast protein liquid chromatography and gel filtration; by fast protein liquid chromatography and gel filtration; by fast protein liquid chromatography and gel filtration
native and recombinant enzyme; recombinant protein; to electrophoretic homogeneity
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partially
recombinant protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli; pheC cloned and expressed by functional complementation of a pheA auxotroph of Escherichia coli
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AtADT1, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview; AtADT2, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview; AtADT3, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview; AtADT4, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview; AtADT5, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview; AtADT6, DNA and amino acid sequence determination and analysis, sequence comparison, complementation of the Saccharomyces cerevisiae pha2 mutant strain YNL316c, which lacks PDT activity and cannot grow in the absence of exogenous Phe by the six ADTs from Arabidopsis thaliana: AtADT2 readily recovers the pha2 phenotype after about 6 days growth at 30C, while AtADT1 requires about 13 days to show visible growth. By contrast, AtADT6, with lowest PDT activity, and AtADT3-5, with no PDT activity, are unable to recover the phenotype, overview
coding regions corresponding to mature ADT protein (lacking the N-terminal plastid transit peptides) subcloned into the expression vector pET-28a, which contains an N-terminal 6xHis tag. Recombinant protein expressed in Escherichia coli Rosetta cells; coding regions corresponding to mature ADT protein (lacking the N-terminal plastid transit peptides) subcloned into the expression vector pET-28a, which contains an N-terminal 6xHis tag. Recombinant protein expressed in Escherichia coli Rosetta cells; coding regions corresponding to mature ADT protein (lacking the N-terminal plastid transit peptides) subcloned into the expression vector pET-28a, which contains an N-terminal 6xHis tag. Recombinant protein expressed in Escherichia coli Rosetta cells
expression in Escherichia coli
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genes adt1-adt6, complementation of the adt5 KO line with ADT5 gene expression under the control of its native promoter or the cauliflower mosaic virus 35S promoter
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overexpression of the mutant gene in rice calli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADT1 exhibits the highest level of expression in corolla and tube, the scentproducing parts of petunia flowers. In corolla, the ADT1 transcript levels exceed those of ADT2 and ADT3 by 88- and 10fold, respectively. ADT1 expression is positively correlated with endogenous Phe levels throughout flower development; in corolla, the ADT1 transcript levels exceed those of ADT2 and ADT3 by 88- and 10fold, respectively; in corolla, the ADT1 transcript levels exceed those of ADT2 and ADT3 by 88- and 10fold, respectively
ADT1 suppression via RNA interference in petunia petals significantly reduces ADT activity, levels of Phe, and downstream phenylpropanoid/benzenoid volatiles, whereby arogenate levels are unaltered, while shikimate and Trp levels are decreased in transgenic petals
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S298I
mutant Mtr1
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
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fine tuning of the feedback sensitivity of ADT may be effective to establish a line that accumulate Phe at a high concentration
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