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L-arogenate
L-phenylalanine + CO2 + H2O
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
prephenate
?
-
-
-
-
?
prephenate
?
-
biosynthesis of phenylalanine
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
activated G-protein Ga-subunit (GPA1) is directly responsible for the activation of PD1. GCR1, GPA1, and PD1 form all of or part of a signal transduction mechanism responsible for the light-mediated synthesis of phenylpyruvate, Phe, and those metabolites that derive from that Phe
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
spectrophotometric assay by measuring the appearance of phenylpyruvate
-
-
?
prephenate
phenylpyruvate + H2O + CO2
the enzyme is involved in aromatic amino acid biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
?
prephenate
phenylpyruvate + H2O + CO2
involved in vivo production of high levels of phenylalanine
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
involved in biosynthesis of L-phenylalanine
-
?
prephenate
phenylpyruvate + H2O + CO2
-
the enzyme is a bifunctional chorismate mutase/prephenate dehydratase which also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, catalyzes the first to steps in the biosynthesis of L-Phe and L-Tyr
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
the enzyme is a bifunctional chorismate mutase/prephenate dehydratase which also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate. L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
13C isotope effect for conversion of prephenate is 1.0334, the size of this isotope effect suggests that the reaction is concerted. Only residue capable of acting as the general acid needed for removal of the hydroxyl group is threonine-172, which is contained in a conserved TRF motif. More favorable entropy of activation for the enzyme-catalyzed process (25 eu larger than for the acid-catalyzed reaction) may be due to preorganized microenvironment that obviates the need for extensive solvent reorganization, which is consistent with forced planarity of the ring and side chain, which may place the leaving carboxyl and hydroxyl out of plane. Such distortion of the substrate may be a major contributor to catalysis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
first enzyme in the phenylalanine biosynthesis branch of the biosynthetic pathway for aromatic amino acids
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
key regulator enzyme in L-phenylalanine biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
the enzyme is absolutely dependent on the presence of catalytic as well as the regulatory domains for optimum enzyme activity. The enzyme is monofunctional and does not possess any chorismate mutase activity
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
prephenate dehydratase part of trifunctional enzyme
-
-
?
prephenate
phenylpyruvate + H2O + CO2
bifunctional enzyme, PDT activity with prephenate and ADT activity with arogenate
-
-
?
prephenate
phenylpyruvate + H2O + CO2
bifunctional enzyme, prephenate dehydratase-arogenate dehydratase, preference for arogenate as substrate indicates primary function as an arogenate dehydratase (ADT)
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
at the interface two ACT regulatory domains create two highly conserved pockets. Upon binding of the L-Phe inside the pockets, PDT transits from an open to a closed conformation
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
-
-
?
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0.32
-
mutant F185Y, pH 7.5, 30°C
0.39
-
mutant T183S, pH 7.5, 30°C
18.2
-
crude native cell extract
18000
strain WSH-Z06 (pAP-B03)
18600
strain WSH-Z06 (pAP-B01)
2.37
-
mutant S99A, pH 7.5, 30°C
3100
strain WSH-Z06 (pAP-B)
37.6
-
purified recombinant prephenate dehydratase domain
4.31
-
mutant R184L, pH 7.5, 30°C
40.4
-
purified recombinant mutant E159A
42.9
-
purified recombinant mutant E232A
56.9
-
purified recombinant double mutant E159A/E232A
6.66
-
mutant S99M, pH 7.5, 30°C
6.88
-
mutant S99C, pH 7.5, 30°C
7.59
-
mutant S99T, pH 7.5, 30°C
8.1
-
mutant E164D, pH 7.5, 30°C
9.48
-
wild-type enzyme, pH 7.5, 30°C
additional information
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities, prephenate dehydratase activity spectrophotometric quantified by monitoring the appearance of phenylpyruvate at 320 nm in end-point assays
additional information
-
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities, prephenate dehydratase activity spectrophotometric quantified by monitoring the appearance of phenylpyruvate at 320 nm in end-point assays
additional information
-
seasonal clonal variations, and effects of stresses and leaf age on prephenate dehydratase enzyme activity in different tea samples, overview
additional information
-
substrate specificity of the bifunctional enzyme, activity of mutant enzymes, overview
additional information
three-dimensional enzyme structure, oligomeric state determined, circular dichroism method and bioinformatics tools, hydrodynamic properties, analytical ultracentrifugation experiments, small angle X-ray scattering, enzyme stability shown by molecular dynamics simulations, predicted as a flat disk protein with an asymmetric shape
additional information
-
three-dimensional enzyme structure, oligomeric state determined, circular dichroism method and bioinformatics tools, hydrodynamic properties, analytical ultracentrifugation experiments, small angle X-ray scattering, enzyme stability shown by molecular dynamics simulations, predicted as a flat disk protein with an asymmetric shape
additional information
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities
additional information
-
trifunctional enzyme containing prephenate dehydratase (PDT), also chorismate mutase (CM, 5.4.99.5), and prephenate dehydrogenase (PDHG, 1.3.1.12) acitivities
additional information
Mtr1 mutant of rice indicates accumulation of L-phenylalanine, L-trytophan, and of several phenylpropanoids, suggesting a link between the synthesis of L-phenylalanine and L-trytophan, mtr1-D mutant gene indicates point mutation in the putative allosteric regulatory region, wild-type enzyme is feedback regulated by L-phenylalanine, Mtr1 mutant has reduced feedback activity and accumulates L-phenylalanine, critical for regulating the size of the pool of L-phenylalanine in plant cells
additional information
Mtr1 mutant of rice indicates accumulation of L-phenylalanine, L-trytophan, and of several phenylpropanoids, suggesting a link between the synthesis of L-phenylalanine and L-trytophan, mtr1-D mutant gene indicates point mutation in the putative allosteric regulatory region, wild-type enzyme is feedback regulated by L-phenylalanine, Mtr1 mutant has reduced feedback activity and accumulates L-phenylalanine, critical for regulating the size of the pool of L-phenylalanine in plant cells
additional information
-
Mtr1 mutant of rice indicates accumulation of L-phenylalanine, L-trytophan, and of several phenylpropanoids, suggesting a link between the synthesis of L-phenylalanine and L-trytophan, mtr1-D mutant gene indicates point mutation in the putative allosteric regulatory region, wild-type enzyme is feedback regulated by L-phenylalanine, Mtr1 mutant has reduced feedback activity and accumulates L-phenylalanine, critical for regulating the size of the pool of L-phenylalanine in plant cells
additional information
comparison of prephenate dehydratase isolated from Zymomonas mobilis to those of Escherichia coli with regard to the capacity to produce L-tyrosine in Escherichia coli strains modified to increase the carbon flow to chorismate, kinetic and stoichiometric parameters determined in shake flask experiments, parameters determined from data generated in bioreactor experiments, possibility to employ feedback inhibition-insensitive enzymes for strain development as part of a metabolic engineering strategy for L-tyrosine production
additional information
-
comparison of prephenate dehydratase isolated from Zymomonas mobilis to those of Escherichia coli with regard to the capacity to produce L-tyrosine in Escherichia coli strains modified to increase the carbon flow to chorismate, kinetic and stoichiometric parameters determined in shake flask experiments, parameters determined from data generated in bioreactor experiments, possibility to employ feedback inhibition-insensitive enzymes for strain development as part of a metabolic engineering strategy for L-tyrosine production
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E64D
-
constructed by PCR-based random mutagenesis and complementation analysis, 15% reduced activity compared to the wild-type enzyme, 4.5% increased Km, 1.7fold increased kcat
E64Q
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
E64S
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
E64V
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
F185L
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
F185Y
-
constructed by PCR-based random mutagenesis and complementation analysis, 96% reduced activity compared to the wild-type enzyme, 26% increased Km
R184L
-
constructed by PCR-based random mutagenesis and complementation analysis, 50% reduced activity compared to the wild-type enzyme
S99A
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99C
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99L
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
S99M
-
constructed by PCR-based random mutagenesis and complementation analysis, 30% reduced activity compared to the wild-type enzyme, insensitive to inhibition by phenylalanine
T183A
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
T183S
-
constructed by PCR-based random mutagenesis and complementation analysis, highly reduced activity
T183Y
-
constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant
S99A
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
-
S99C
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
-
S99L
-
constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine
-
S99M
-
constructed by PCR-based random mutagenesis and complementation analysis, 30% reduced activity compared to the wild-type enzyme, insensitive to inhibition by phenylalanine
-
C216A
-
site-directed mutagenesis, inactive mutant
C216S
-
site-directed mutagenesis, increased activity
E159A
-
site-directed mutagenesis, 2.2fold increased activity
E159A/E232A
-
site-directed mutagenesis, 7fold increased kcat, 4.6fold decreased Km compared to the wild-type, increased activity
E232A
-
site-directed mutagenesis, 3.5fold increased activity
H209A
-
site-directed mutagenesis, highly reduced activity
N160A
-
site-directed mutagenesis, 500fold decreased activity
N160D
-
site-directed mutagenesis, highly reduced activity
Q215A
-
site-directed mutagenesis, 500fold decreased activity
S208A
-
site-directed mutagenesis, 100fold decreased activity
S208C
-
site-directed mutagenesis, 100fold decreased activity
S208D
-
site-directed mutagenesis, inactive mutant
T278A
-
site-directed mutagenesis, catalytically inactive mutant, but binds to substrate and inhibitor
T278S
-
site-directed mutagenesis, 100fold decreased activity
T278V
-
site-directed mutagenesis, catalytically inactive mutant, but binds to substrate and inhibitor
T326P
mutant harboring pheAfbr retains more than 70% of CM and PDT activities even in the presence of 200 mM L-phenylalanine, has potential in overproduction of L-phenylalanine
W226A
-
site-directed mutagenesis, nearly inactive mutant
W226L
-
site-directed mutagenesis, highly reduced activity
T326P
-
mutant harboring pheAfbr retains more than 70% of CM and PDT activities even in the presence of 200 mM L-phenylalanine, has potential in overproduction of L-phenylalanine
-
additional information
-
alterations of Asp76, Glu89, His115, and Arg236 do not cause significant changes in the kinetics properties
additional information
-
alterations of Asp76, Glu89, His115, and Arg236 do not cause significant changes in the kinetics properties
-
additional information
-
production of inhibitor-insensitive mutants
additional information
-
expression of genes contaninig P-protein domains or subdomains, comparison of their catalytic activities and activation by phenylalanine
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Friedrich, B.; Friedrich, C.G.; Schlegel, H.G.
Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus
J. Bacteriol.
126
712-722
1976
Cupriavidus necator
brenda
Gething, M.J.; Davidson, B.E.; Dopheide, T.A.A.
Chorismate mutase/prephenate dehydratase from Escherichia coli K12. 1. The effect of NaCl and its use in a new purification involving affinity chromatography on sepharosyl-phenylalanine
Eur. J. Biochem.
71
317-325
1976
Escherichia coli
brenda
Stewart, J.; Wilson, D.B.; Ganem, B.
Chorismate mutase/prephenate dehydratase from Escherichia coli: subcloning, overproduction and purification
Tetrahedron
47
2573-2577
1991
Escherichia coli
-
brenda
Ahmad, S.; Wilson, A.T.; Jensen, R.A.
Chorismate mutase: prephenate dehydratase from Acinetobacter calcoaceticus. Purification, properties and immunological cross-reactivity
Eur. J. Biochem.
176
69-79
1988
Acinetobacter calcoaceticus
brenda
Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D.B.; Clardy, J.; Ganem, B.
Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins
J. Biol. Chem.
273
6248-6253
1998
Escherichia coli
brenda
Davidson, B.E.
Chorismate mutase-prephenate dehydratase from Escherichia coli
Methods Enzymol.
142
432-439
1987
Escherichia coli
brenda
Bertaux, S.; Harrison, R.G.
Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography
Prep. Biochem.
21
269-275
1991
Corynebacterium glutamicum
brenda
Jensen, R.A.; d'Amato, T.A.; Hochstein, L.I.
An extreme-halophile archaebacterium possesses the interlock type or prephenate dehydratase characteristic of gram-positive eubacteria
Arch. Microbiol.
148
365-371
1988
Haloarcula vallismortis
brenda
Fischer, R.; Jensen, R.
Prephenate dehydratase (monofunctional)
Methods Enzymol.
142
507-512
1987
Bacillus subtilis
brenda
Follettie, M.T.; Sinskey, A.J.
Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene
J. Bacteriol.
167
695-702
1986
Corynebacterium glutamicum
brenda
Ozaki, A.; Katsumata, R.; Oka, T.; Furuya, A.
Cloning of the genes concerend in phenylalanine biosynthesis in Corynebacterium glutamicum and its application to breeding of a phenylalanine producing strain
Agric. Biol. Chem.
49
2925-2930
1985
Corynebacterium glutamicum
-
brenda
Bode, R.; Melo, C.; Birnbaum, D.
Regulation of chorismate mutase, prephenate dehydrogenase and prephenate dehydratase of Candida maltosa
J. Basic Microbiol.
25
291-298
1985
Candida maltosa
-
brenda
Baldwin, G.S.; Davidson, B.E.
Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12
Biochim. Biophys. Acta
742
374-383
1983
Escherichia coli
brenda
Baldwin, G.S.; McKenzie, G.H.; Davidson, B.E.
The self-association of chorismate mutase/prephenate dehydratase from Escherichia coli K12
Arch. Biochem. Biophys.
211
76-85
1981
Escherichia coli
brenda
Krauss, G.; Suessmuth, R.; Lingens, F.
[A prephenate dehydratase from Flavobacterium devorans stimulated by aromatic amino acids (author s transl)
Hoppe-Seyler's Z. Physiol. Chem.
361
809-818
1980
Sphingomonas paucimobilis
brenda
Riepl, R.G.; Glover, G.I.
Regulation and state of aggregation of Bacillus subtilis prephenate dehydratase in the presence of allosteric effectors
J. Biol. Chem.
254
10321-10328
1979
Bacillus subtilis
brenda
Riepl, R.G.; Glover, G.I.
Purification of Prephenate dehydratase from Bacillus subtilis
Arch. Biochem. Biophys.
191
192-197
1978
Bacillus subtilis
brenda
Friedrich, C.G.; Friedrich, B.; Schlegel, H.G.
Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus
J. Bacteriol.
126
723-732
1976
Cupriavidus necator
brenda
Hagino, H.; Nakayama, K.
Regulatory properties of prephenate dehydrogenase and prephenate dehydratase from Corynebacterium glutamicum
Agric. Biol. Chem.
38
2367-2376
1974
Corynebacterium glutamicum
-
brenda
Dopheide, T.A.A.; Crewther, P.; Davidson, B.E.
Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties
J. Biol. Chem.
247
4447-4452
1972
Escherichia coli
brenda
Davidson, B.E.; Blackburn, E.H.; Dopheide, T.A.A.
Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. I. Purification, molecular weight, and amino acid composition
J. Biol. Chem.
247
4441-4446
1972
Escherichia coli
brenda
Schmit, J.C.; Artz, S.W.; Zalkin, H.
Chorismate mutase-prephenate dehydratase. Evidence for distinct catalytic and regulatory sites
J. Biol. Chem.
245
4019-4027
1970
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Schmit, J.C.; Zalkin, H.
Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium
Biochemistry
8
174-181
1969
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cerutti, P.; Guroff, G.
Enzymatic formation of phenylpyruvic acid in Pseudomonas sp. (ATCC11299a) and its regulation
J. Biol. Chem.
240
3034-3038
1965
Pseudomonas sp.
brenda
Bushweller, J.H.; Bartlett, P.A.
Sulfoxide analogues of dihydro- and tetrahydroprephenate as inhibitors of prephenate dehydratase
J. Org. Chem.
54
2404-2409
1989
Escherichia coli
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