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Information on EC 4.2.1.51 - prephenate dehydratase
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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
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-
-
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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
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-
-
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dehydratase, prephenate
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-
-
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monofunctional prephenate dehydratase
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-
-
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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)
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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)
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P-protein
-
-
-
-
PDT
-
-
-
-
PDT
bifunctional enzyme, PDT activity with prephenate and ADT activity with arogenate
PheA
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the bifunctional PheA protein contains two catalytic domains (chorismate mutase and prephenate dehydratase activities)
PheA
Escherichia coli W3110 / ATCC 27325
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the bifunctional PheA protein contains two catalytic domains (chorismate mutase and prephenate dehydratase activities)
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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
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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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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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-
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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
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-
?
prephenate
phenylpyruvate + H2O + CO2
the enzyme is involved in aromatic amino acid biosynthesis
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-
?
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
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-
?
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
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-
?
prephenate
phenylpyruvate + H2O + CO2
-
first enzyme in the phenylalanine biosynthesis branch of the biosynthetic pathway for aromatic amino acids
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-
?
prephenate
phenylpyruvate + H2O + CO2
-
key regulator enzyme in L-phenylalanine biosynthesis
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-
?
prephenate
phenylpyruvate + H2O + CO2
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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
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-
?
prephenate
phenylpyruvate + H2O + CO2
prephenate dehydratase part of trifunctional enzyme
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-
?
prephenate
phenylpyruvate + H2O + CO2
bifunctional enzyme, PDT activity with prephenate and ADT activity with arogenate
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-
?
prephenate
phenylpyruvate + H2O + CO2
bifunctional enzyme, prephenate dehydratase-arogenate dehydratase, preference for arogenate as substrate indicates primary function as an arogenate dehydratase (ADT)
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-
?
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
L-methionine