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Information on EC 4.2.1.51 - prephenate dehydratase
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EC Tree
4.2.1.51 prephenate dehydrataseIUBMB Comments
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
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Word Map
- 4.2.1.51
- l-phenylalanine
- arogenate
- l-tyrosine
- dahp
- l-phe
- 7-phosphate
-
cyclohexadienyl
- l-tyr
-
3-deoxy-d-arabino-heptulosonate
-
feedback-inhibited
-
5.4.99.5
- synthesis
- industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
prephenate dehydratase, chorismate mutase-prephenate dehydratase, chorismate mutase prephenate dehydratase, cm-pd, mtbpdt, pdt protein, monofunctional prephenate dehydratase, mjpdt, sa-pdt, ct-pdt, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADT1
-
the arogenate dehydratase isoform has limited activity with prephenate
ADT2
-
the arogenate dehydratase isoform has limited activity with prephenate
ADT6
-
the arogenate dehydratase isoform has limited activity with prephenate
AroQ
gene name. Trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase)
chorismate mutase prephenate dehydratase
chorismate mutase-prephenate dehydratase
Chorismate mutase/prephenate dehydratase
CM-PD
-
-
-
-
CM/PDT/PDHG
trifunctional enzyme EC 5.4.99.5 (chorismate mutase)/EC 4.2.1.51 (prephenate dehydratase)/EC 1.3.1.12 (prephenate dehydrogenase)
CMPDT
cyclohexydienyl dehydratase
-
-
-
-
dehydratase, prephenate
-
-
-
-
monofunctional prephenate dehydratase
-
-
-
-
MtbPDT
P-protein
PDT
PDT protein
PheA
prephenate dehydratase
chorismate mutase-prephenate dehydratase
the enzyme also possesses chorismate mutase activity (EC 5.4.99.5)
chorismate mutase-prephenate dehydratase
the enzyme also possesses chorismate mutase activity (EC 5.4.99.5)
-
CMPDT
the enzyme also possesses chorismate mutase activity (EC 5.4.99.5)
CMPDT
the enzyme also possesses chorismate mutase activity (EC 5.4.99.5)
-
P-protein
-
-
-
-
PDT
-
-
-
-
PDT
bifunctional enzyme, PDT activity with prephenate and ADT activity with arogenate
PheA
-
the bifunctional PheA protein contains two catalytic domains (chorismate mutase and prephenate dehydratase activities)
PheA
Escherichia coli W3110 / ATCC 27325
-
the bifunctional PheA protein contains two catalytic domains (chorismate mutase and prephenate dehydratase activities)
-
prephenate dehydratase
bifunctional enzyme, PDT activity with prephenate and ADT activity with arogenate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prephenate = phenylpyruvate + H2O + CO2
-
-
-
-
prephenate = phenylpyruvate + H2O + CO2
this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate
prephenate = phenylpyruvate + H2O + CO2
this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, catalytic mechanism, T278 is involved in catalysis
-
prephenate = phenylpyruvate + H2O + CO2
this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, residues Glu64, Thr183, Arg184, and Phe185 might be involved in catalysis and substrate binding
-
prephenate = phenylpyruvate + H2O + CO2
this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, residues Glu64, Thr183, Arg184, and Phe185 might be involved in catalysis and substrate binding
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
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CAS REGISTRY NUMBER
COMMENTARY
9044-88-6
-
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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
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
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
involved in vivo production of high levels of phenylalanine
-
?
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
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
prephenate
phenylpyruvate + H2O + CO2
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
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
-
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
-
first enzyme in the phenylalanine biosynthesis branch of the biosynthetic pathway for aromatic amino acids
-
-
?
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 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
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
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
the enzyme is involved in aromatic amino acid biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
involved in vivo production of high levels of phenylalanine
-
?
prephenate
phenylpyruvate + H2O + CO2
-
converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
prephenate
phenylpyruvate + H2O + CO2
-
enzyme is a key regulatory enzyme in the phenylalanine-specific pathway
-
?
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
-
first enzyme in the phenylalanine biosynthesis branch of the biosynthetic pathway for aromatic amino acids
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
key regulator enzyme in L-phenylalanine biosynthesis
-
-
?
prephenate
phenylpyruvate + H2O + CO2
-
converts prephenate to phenylpyruvate in L-phenylalanine biosynthesis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-phenylalanine
inhibits activity at 5 microM, competitive inhibition
L-phenylalanine
-
feedback inhibition, Ser99 is involved, mutants S99M, S99T, S99A, S99C, or S99L are not sensitive to inhibition
L-phenylalanine
feedback inhibition. PDT of Escherichia coli WSH-Z06 is almost completely inhibited by 10 mM L-phenylalanine (92.9% activity loss). PDT of Escherichia coli WSH-Z06 (pAP-B03) exhibits strong resistance to 200 mM L-phenylalanine, manifested by the high residual activities (10 mM L-phenylalanine with only 7.1% loss of activity)
L-phenylalanine
feedback regulation wild-type, mutant enzyme MTR1 (PDT S298I) shows a reduced feedback sensitivity, resulting in phenylalanine accumulation; inhibits activity of wild-type enzyme, mutant enzyme shows reduced feedback sensitivity, accumulation of L-phenylalanine
NaCl
-
enzyme activity is completely abolished in the presence of 200 mM and higher concentrations of NaCl
additional information
changes in the ESRP sequence, involved in allosteric binding of phenylalanine, lead to desensitization to inhibition by phenylalanine, permitting the overproduction of the amino aid in vivo
-
additional information
-
changes in the ESRP sequence, involved in allosteric binding of phenylalanine, lead to desensitization to inhibition by phenylalanine, permitting the overproduction of the amino aid in vivo
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Crystallization and preliminary X-ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv.
Tuberculosis
pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity.
Tuberculosis
Structural studies of prephenate dehydratase from Mycobacterium tuberculosis H37Rv by SAXS, ultracentrifugation, and computational analysis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km for chorismate of wild-type and mutants
-
1.3
phenylpyruvate
measuring the appearance of phenylpyruvate at 320 nm, performed with 1 mM prephenate in 200 mM Tris buffer
0.3
prephenate
pH 8.0, 37°C, prephenate dehydratase Cmut1
1.2
prephenate
-
pH and temperature not specified in the publication
2.11
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut11
2.15
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut9
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat for chorismate of wild-type and mutants
-
0.031
prephenate
pH 8.0, 37°C, prephenate dehydratase Cmut1
0.036
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut11
0.04
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut9
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.14
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut11
18.6
prephenate
pH 8.0, 37°C, prephenate dehydratase Gmut9
103.3
prephenate
pH 8.0, 37°C, prephenate dehydratase Cmut1
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
61.5
L-phenylalanine
mutant enzyme S298I, rice PDT is a bifunctional enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
L-phenylalanine
Oryza sativa
wild-type, rice PDT is a bifunctional enzyme
additional information
additional information
Oryza sativa
L-phenylalanine more than 0.5
-
additional information
additional information
Oryza sativa
L-phenylalanine more than 0.5
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.5
spectrophotometric assay performed at several different pH values
6.2 - 9
-
86% of maximal activity at pH 6.2, 65% of maximal activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
77
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
endosymbiont isolated from aphid Acyrthosiphon pisum
SwissProt
brenda
tea clones representing both Assam and China varieties growing in Kangra region of India
-
-
brenda
the enzyme possesses prephenate dehydratase (EC 4.2.1.51) and chorismate mutase activity (EC 5.4.99.5); K06
UniProt
brenda
encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
SwissProt
brenda
encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
SwissProt
brenda
-
-
-
brenda
the enzyme possesses prephenate dehydratase (EC 4.2.1.51) and chorismate mutase activity (EC 5.4.99.5); K06
UniProt
brenda
encoded by pheA gene (Rv3838c); H37Rv
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
wild-type, and transformed callus lines expressing mtr1-D mutation, experimental system for feeding experiments with external L-phenylalanine
brenda
feeding experiments with external L-phenylalanine, accumulation of L-trytophan
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
all plant clades include PAC domain-containing arogenate dehydratases, suggesting that the prephenate dehydratase activity, and thus the ability to synthesize L-phenylalanine using phenylpyruvate as an intermediate, has been preserved throughout the evolution of plants. This pathway together with the arogenate pathway gives plants a broad and versatile capacity to synthesize L-phenylalanine and its derived compounds
malfunction
metabolism
physiological function
additional information
-
a decrease in catechins content, 2-phenylethanol, and PDT activity is observed in the tea shoots infested by Exobasidium vexans over healthy shoots. Drought stress induced by withholding water for a period of 8 days causes initial increase in the contents of the catechins and 2-phenylethanol, and in PDT activity, but decreases with 3 day onwards with an increase in the severity of water stress, detailed overview
malfunction
use of a T326P mutation in the regulation domain of pheA (pheAfbr) for L-phenylalanine production. Overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis
malfunction
-
use of a T326P mutation in the regulation domain of pheA (pheAfbr) for L-phenylalanine production. Overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis
-
metabolism
-
transgenic Arabidopsis plants expressing a truncated, feedback-insensitive chorismate mutase/prephenate dehydratase gene accumulate Phe (up to 100fold compared to control plants) and are more sensitive than wild-type plants to the Trp biosynthesis inhibitor 5-methyl-Trp. Thus Phe biosynthesis competes with Trp biosynthesis from their common precursor chorismate. A number of secondary metabolites derived from all three aromatic amino acids (Phe, Trp and Tyr) are altered in the transgenic plants, implying regulatory cross-interactions between the flux of aromatic amino acid biosynthesis from chorismate and their further metabolism into various secondary metabolites. Truncated PheA expression has a minimal effect on primary metabolism and on the Arabidopsis transcriptome. A high proportion of the feedback-insensitive chorismate mutase/prephenate dehydratase polypeptide produced by this transgene is translocated into the plastids
metabolism
-
prephenate dehydratase takes part in the biosynthetic pathway of flavan-3-ols, overview
metabolism
the enzyme is involved in aromatic amino acid biosynthesis
metabolism
the enzyme is involved in L-phenylalanine biosynthesis pathway
metabolism
the enzyme is involved in the phenylpyruvate biosynthetic pathway
physiological function
Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
physiological function
-
involved in aromatic amino acid metabolism
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
175000
-
bifunctional enzyme, chorismate mutase:prephenate dehydratase, presence of L-Phe, gel filtration
18000
-
4 * 18000, bifunctional enzyme prephenate dehydratase-arogenate dehydratase, SDS-PAGE
28300
35000
39000
-
x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE
40000
43111
55000
73000
-
bifunctional enzyme, prephenate dehydratase-arogenate dehydratase, gel filtration
90000 - 273000
-
ultracentrifugation at various experimental conditions, depending on pH, temperature, salt concentration, protein concentration the enzyme undergoes self-association
91000
-
bifunctional enzyme, chorismate mutase:prephenate dehydratase, absence of L-Phe, gel filtration
35000
processed to a product of 35000 Dalton during incubation with pea chloroplasts, protected from degradation by thermolysin, organellar targeting sequence
35000
-
2 * 35000, low activity in absence of activators, high activity in presence of activators
43111
-
2 * 43111, smallest native species of enzyme, calculation from nucleotide sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homohexamer
homotetramer
octamer
oligomer
-
L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
tetramer
additional information
-
the enzyme consists of 3 domains: a chorismate mutase domain, a prephenate dehydratase domain, and a regulatory domain
?
-
x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE
-
dimer
-
2 * 35000, low activity in absence of activators, high activity in presence of activators
dimer
-
2 * 43111, smallest native species of enzyme, calculation from nucleotide sequence
dimer
-
L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
homotetramer
determined by small angle X-ray scattering and analytical ultracentrifugation
homotetramer
-
determined by small angle X-ray scattering and analytical ultracentrifugation
-
tetramer
-
L-Phe binds with positive cooperativity and the binding shifts the protein from dimeric to less active tetrameric and higher oligomeric forms
tetramer
-
4 * 18000, bifunctional enzyme prephenate dehydratase-arogenate dehydratase, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapour-diffusion method using PEG 400 as a precipitant. The crystal belongs to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 98.26, b = 133.22, c = 225.01 A, and contains four molecules in the asymmetric unit
-
hanging drop vapor diffusion method, using 15% (w/v) polyethylene glycol 8000, 100 mM magnesium chloride, 100 mM Tris-HCl, pH 7.4
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
E159A/E232A
-
site-directed mutagenesis, 7fold increased kcat, 4.6fold decreased Km compared to the wild-type, increased activity
T278A
-
site-directed mutagenesis, catalytically inactive mutant, but binds to substrate and inhibitor
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
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
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
-
expression of genes contaninig P-protein domains or subdomains, comparison of their catalytic activities and activation by phenylalanine
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
absence of activators, 2 min, 60% loss of activity, presence of l-Phe or L-Tyr, 5-7% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
octameric form, whose aggregation is caused by activator molecules is stable, while the dimeric form can be stabilized by glycerol
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C
-20°C, 50 mM phosphate buffer, pH 7.4, 0.7 mg protein/ml, stable for 10 months
-
4°C, 20 mM Tris-HCl, pH 8.2, 1 mM EDTA, 10 mM 2-mercaptoethanol, 0.3 M NaCl, 0.02% w/v NaN3, 1 mM dihiothreitol, 2 weeks stable
-
4°C, 20% glycerol or presence of L-Met, L-Leu, prephenate, stable for several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme, chorismate mutase:prephenate dehydratase
catalytic and regulatory domains of prephenate dehydratase, individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3)
-
Ni-NTA affinity column chromatography, and Superdex 200 gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type prephenate dehydratase domain and the mutant enzymes
-
bifunctional enzyme, chorismate mutase:prephenate dehydratase
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis of the two-domain aroQ/pheA gene, constitutive expression due to the absence of an attenuator region, changes in the ESRP sequence leading to desensitization to inhibition by phenylalanine
expressed in Corynebacterium glutamicum
expressed in different engineered Escherichia coli WSH-Z06 strains (pAP-B, pAP-B01, pAP-B02 and pAP-B03)
expressed in Escherichia coli (DE3)-RIL, pIS85 expression plasmid
expressed in Escherichia coli BL21(DE3), pET-23a(+) expression vector
expressed in Escherichia coli, mtr1-D mutant gene, callus transformation by Agrobacterium tumefaciens
expressed in Escherichia coli, PB12 strain, pCR-BluntII-TOPO, additional strains and plasmids listed
expression of mutant enzymes in enzyme deficient strain NK6024, subcloning in strain DH5alpha, overexpression of the isolated His-tagged wild-type prephenate dehydratase domain in strain BL21(DE3)
-
expression of the His-tagged wild-type and mutant enzymes in Escherichia coli JM109
-
generation of transgenic Arabidopsis plants expressing a bacterial feedback-insensitive chorismate mutase/prephenate dehydratase gene (truncated PheA) under the control of the 35S CaMV promoter, fused inframe at the 3' end of the coding sequence to DNA encoding a hemagglutinin epitope tag. Two chimeric constructs: in one, DNA encoding a Rubisco small subunit-3A plastid transit peptide is fused in-frame to the 5' end of the PheA open reading frame to direct the bacterial enzyme in to the plastid where aromatic amino acid biosynthesis is localized. The second construct lacks the Rubisco small subunit-3A plastid transit peptide in order to test whether aromatic amino acid metabolism is strictly localized to the plastid or whether at least some parts of it operate in the cytosol. Both constructs transformed into Arabidopsis plants, and homozygous T2 plants are generated
-
overexpressed in Escherichia coli KA13, transformed with the plasmid pAKZ11
-
the catalytic and regulatory domains of prephenate dehydratase are individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the presence of aryl acids does not have a large affect on the expression of the enzyme
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
synthesis
industry
overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis, which is an important prerequisite for improved production of L-phenylalanine with engineered strains
industry
-
overexpression of pheAfbr and/or wild-type aroF is helpful for the enhancement of the key enzymes in L-phenylalanine biosynthesis, which is an important prerequisite for improved production of L-phenylalanine with engineered strains
-
synthesis
-
synthesis of L-Phe, pheA gene expressed in Corynebacterium glutamicum
synthesis
synthesis of L-phenylalanine (an important amino acid that is widely used in the production of food flavors and pharmaceuticals) by engineered Escherichia coli. Coexpression of Vitreoscilla hemoglobin gene, driven by a tac promoter, with the genes encoding 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase (aroF) and feedback-resistant chorismate mutase/prephenate dehydratase (pheAfbr), leads to increased productivity of L-phenylalanine and decreased demand for aeration by Escherichia coli CICC10245
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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273
6248-6253
1998
Escherichia coli
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Chorismate mutase-prephenate dehydratase from Escherichia coli
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432-439
1987
Escherichia coli
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Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography
Prep. Biochem.
21
269-275
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Corynebacterium glutamicum
brenda
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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
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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
-
brenda
Xia, T.; Ahmad, S.; Zhao, G.; Jensen, R.A.
A single cyclohexadienyl dehydratase specifies the prephenate dehydratase and arogenate dehydratase components of one of two independent pathways to L-phenylalanine in Erwinia herbicola
Arch. Biochem. Biophys.
286
461-465
1991
Pantoea agglomerans
brenda
Nelms, J.; Edwards, R.M.; Warwick, J.; Fotheringham, I.
Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase
Appl. Environ. Microbiol.
58
2592-2598
1992
Escherichia coli
brenda
Ikeda, M.; Ozaki, A.; Katsumata, R.
Phenylalanine production by metabolically engineered Corynebacterium glutamicum with the pheA gene of Escherichia coli
Appl. Microbiol. Biotechnol.
39
318-323
1993
Escherichia coli
brenda
Vrijbloed, J.W.; Hylckama Vlieg, J.; Put, J.; Hessels, G.I.; Dijkhuizen, L.
Molecular cloning with a pMEA300-derived shuttle vector and characterization of the Amycolatopsis methanolica prephenate dehydratase gene
J. Bacteriol.
177
6666-6669
1995
Amycolatopsis methanolica
brenda
Euverink, G.J.W.; Wolters, D.J.; Dijkhuizen, L.
Prephenate dehydratase of the actinomycete Amycolatopsis methanolica: purification and characterization of wild-type and deregulated mutant proteins
Biochem. J.
308
313-320
1995
Amycolatopsis methanolica
brenda
Chan, M.S.; Hsu, W.H.
Cloning of m-fluorophenylalanine-resistant gene and mutational analysis of feedback-resistant prephenate dehydratase from Corynebacterium glutamicum
Biochem. Biophys. Res. Commun.
219
537-542
1996
Corynebacterium glutamicum
brenda
Fischer, R.S.; Zhao, G.; Jemsen, R.A.
Cloning, sequencing, and expression of the P-protein gene (pheA) of Pseudomonas stutzeri in Escherichia coli: implications for evolutionary relationships in phenylalanine biosynthesis
J. Gen. Microbiol.
137
1293-1301
1991
Pseudomonas stutzeri
brenda
Hsu, S.K.; Lin, L.L.; Lo, H.H.; Hsu, W.H.
Mutational analysis of feedback inhibition and catalytic sites of prephenate dehydratase from Corynebacterium glutamicum
Arch. Microbiol.
181
237-244
2004
Corynebacterium glutamicum, Corynebacterium glutamicum CCRC 11384
brenda
Zhang, S.; Wilson, D.B.; Ganem, B.
Probing the catalytic mechanism of prephenate dehydratase by site-directed mutagenesis of the Escherichia coli P-protein dehydratase domain
Biochemistry
39
4722-4728
2000
Escherichia coli
brenda
Jimenez, N.; Gonzalez-Candelas, F.; Silva, F.J.
Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibition by phenylalanine
J. Bacteriol.
182
2967-2969
2000
Buchnera aphidicola (P57472), Buchnera aphidicola
brenda
Liberles, J.S.; Thorolfsson, M.; Martinez, A.
Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism
Amino Acids
28
1-12
2005
Escherichia coli
brenda
Prakash, P.; Pathak, N.; Hasnain, S.E.
pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity
J. Biol. Chem.
280
20666-20671
2005
Mycobacterium tuberculosis
brenda
Vivan, A.L.; Dias, M.V.; Schneider, C.Z.; Filgueira De Azevedo, W.J.; Basso, L.A.; Santos, D.S.
Crystallization and preliminary X-ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
62
357-360
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Kleeb, A.C.; Kast, P.; Hilvert, D.
A monofunctional and thermostable prephenate dehydratase from the archaeon Methanocaldococcus jannaschii
Biochemistry
45
14101-14110
2006
Methanocaldococcus jannaschii
brenda
Tan, K.; Li, H.; Zhang, R.; Gu, M.; Clancy, S.T.; Joachimiak, A.
Structures of open (R) and close (T) states of prephenate dehydratase (PDT)-implication of allosteric regulation by L-phenylalanine
J. Struct. Biol.
162
94-107
2007
Chlorobaculum tepidum, Staphylococcus aureus
brenda
Warpeha, K.M.; Lateef, S.S.; Lapik, Y.; Anderson, M.; Lee, B.S.; Kaufman, L.S.
G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate dehydratase 1 are required for blue light-induced production of phenylalanine in etiolated Arabidopsis
Plant Physiol.
140
844-855
2006
Arabidopsis thaliana (Q9ZUY3)
brenda
Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
Appl. Environ. Microbiol.
74
3284-3290
2008
Zymomonas mobilis (Q5NLV8), Zymomonas mobilis, Zymomonas mobilis ATCC 31821 (Q5NLV8)
brenda
Lim, S.; Springstead, J.R.; Yu, M.; Bartkowski, W.; Schroeder, I.; Monbouquette, H.G.
Characterization of a key trifunctional enzyme for aromatic amino acid biosynthesis in Archaeoglobus fulgidus
Extremophiles
13
191-198
2009
Archaeoglobus fulgidus (O30012), Archaeoglobus fulgidus, Nanoarchaeum equitans (Q74NC4), Nanoarchaeum equitans
brenda
Yamada, T.; Matsuda, F.; Kasai, K.; Fukuoka, S.; Kitamura, K.; Tozawa, Y.; Miyagawa, H.; Wakasa, K.
Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and tryptophan
Plant Cell
20
1316-1329
2008
Oryza sativa (A8CF65), Oryza sativa (Q6Z3Y3), Oryza sativa
brenda
Vivan, A.L.; Caceres, R.A.; Abrego, J.R.; Borges, J.C.; Ruggiero Neto, J.; Ramos, C.H.; de Azevedo, W.F.; Basso, L.A.; Santos, D.S.
Structural studies of prephenate dehydratase from Mycobacterium tuberculosis H37Rv by SAXS, ultracentrifugation, and computational analysis
Proteins
72
1352-1362
2008
Mycobacterium tuberculosis (P9WIC3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIC3), Mycobacterium tuberculosis H37Rv
brenda
Van Vleet, J.; Kleeb, A.; Kast, P.; Hilvert, D.; Cleland, W.W.
13C isotope effect on the reaction catalyzed by prephenate dehydratase
Biochim. Biophys. Acta
1804
752-754
2010
Methanocaldococcus jannaschii
brenda
Zhou, H.; Liao, X.; Wang, T.; Du, G.; Chen, J.
Enhanced l-phenylalanine biosynthesis by co-expression of pheA(fbr) and aroF(wt)
Biores. Technol.
101
4151-4156
2010
Escherichia coli (C7EXK8), Escherichia coli, Escherichia coli K06 (C7EXK8)
brenda
Tzin, V.; Malitsky, S.; Aharoni, A.; Galili, G.
Expression of a bacterial bi-functional chorismate mutase/prephenate dehydratase modulates primary and secondary metabolism associated with aromatic amino acids in Arabidopsis
Plant J.
60
156-167
2009
Escherichia coli
brenda
Battilana, J.; Costantini, L.; Emanuelli, F.; Sevini, F.; Segala, C.; Moser, S.; Velasco, R.; Versini, G.; Stella Grando, M.
The 1-deoxy-D: -xylulose 5-phosphate synthase gene co-localizes with a major QTL affecting monoterpene content in grapevine
Theor. Appl. Genet.
118
653-669
2009
Vitis vinifera x Vitis vinifera, Vitis vinifera x Vitis riparia
brenda
Sharma, V.; Joshi, R.; Gulati, A.
Seasonal clonal variations and effects of stresses on quality chemicals and prephenate dehydratase enzyme activity in tea (Camellia sinensis)
Eur. Food Res. Technol.
232
307-317
2011
Camellia sinensis
brenda
Bross, C.D.; Corea, O.R.; Kaldis, A.; Menassa, R.; Bernards, M.A.; Kohalmi, S.E.
Complementation of the pha2 yeast mutant suggests functional differences for arogenate dehydratases from Arabidopsis thaliana
Plant Physiol. Biochem.
49
882-890
2011
Arabidopsis thaliana
brenda
Porat, I.; Waters, B.W.; Teng, Q.; Whitman, W.B.
Two biosynthetic pathways for aromatic amino acids in the archaeon Methanococcus maripaludis
J. Bacteriol.
186
4940-4950
2004
Methanococcus maripaludis
brenda
Shin, M.H.; Ku, H.K.; Song, J.S.; Choi, S.; Son, S.Y.; Kim, H.D.; Kim, S.K.; Park, I.Y.; Lee, S.J.
X-ray structure of prephenate dehydratase from Streptococcus mutans
J. Microbiol.
52
490-495
2014
Streptococcus mutans (Q8DUV6), Streptococcus mutans
brenda
Liu, S.; Xiao, M.; Zhang, L.; Xu, J.; Ding, Z.; Gu, Z.; Shi, G.
Production of L-phenylalanine from glucose by metabolic engineering of wild type Escherichia coli W3110
Process Biochem.
48
413-419
2013
Escherichia coli, Escherichia coli W3110 / ATCC 27325
-
brenda
Wu, W.B.; Guo, X.L.; Zhang, M.L.; Huang, Q.G.; Qi, F.; Huang, J.Z.
Enhancement of L-phenylalanine production in Escherichia coli by heterologous expression of Vitreoscilla hemoglobin
Biotechnol. Appl. Biochem.
65
476-483
2018
Escherichia coli (C7EXK8)
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El-Azaz, J.; de la Torre, F.; Avila, C.; Canovas, F.M.
Identification of a small protein domain present in all plant lineages that confers high prephenate dehydratase activity
Plant J.
87
215-229
2016
Pinus pinaster, Pinus pinaster (A0A1I9WKA1), Pinus pinaster (A0A1I9WKA2), Pinus pinaster (A0A1I9WKA6)
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Release 2023.1 (January 2023)
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