Information on EC 4.2.1.51 - prephenate dehydratase

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

EC NUMBER
COMMENTARY hide
4.2.1.51
-
RECOMMENDED NAME
GeneOntology No.
prephenate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
prephenate = phenylpyruvate + H2O + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
dehydration coupled with decarboxylation
dehydration
dehydration coupled with decarboxylation
elimination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-phenylalanine biosynthesis I
-
-
L-phenylalanine biosynthesis III (cytosolic, plants)
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
phenylalanine metabolism
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9044-88-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
endosymbiont isolated from aphid Acyrthosiphon pisum
SwissProt
Manually annotated by BRENDA team
tea clones representing both Assam and China varieties growing in Kangra region of India
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CCRC 11384
-
-
Manually annotated by BRENDA team
the enzyme possesses prephenate dehydratase (EC 4.2.1.51) and chorismate mutase activity (EC 5.4.99.5); K06
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC 11299a
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
SwissProt
Manually annotated by BRENDA team
encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate
?
show the reaction diagram
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
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
prephenate
?
show the reaction diagram
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
potassium phosphate
-
1.4-2 M, activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-methyl-DL-tyrosine
-
1 mM, 23% inhibition
3-phenylpropanoate
-
-
4-methyltryptophan
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-Fluorotryptophan
-
-
5-Methyltryptophan
-
-
6-Fluorotryptophan
-
-
alpha-oxo-1-carboxy-4-tetrahydrothiopyranpropanoic acid S-oxide
-
-
alpha-oxo-1-carboxy-5,6-dihydrothiopyranpropanoic acid S-oxide
-
-
cis-aconitate
-
-
citrate
-
-
Cu2+
-
0.1 mM, 100% inhibition
D-tryptophan
-
-
Fe2+
-
0.1 mM, 85% inhibition
Hg2+
-
0.1 mM, 94% inhibition
L-Phe
L-phenylalanine
L-Trp
-
at concentration up to 0.1 mM
L-tryptophan
L-Tyr
-
at concentration up to 0.1 mM
L-tyrosine
-
1 mM, 66% inhibition
m-Chlorophenylalanine
-
-
m-Fluorophenylalanine
m-hydroxyphenylalanine
-
-
N-carbobenzoxyphenylalanine
-
-
-
N-ethylmaleimide
-
-
Ni2+
-
0.1 mM, 83% inhibition
o-Chlorophenylalanine
-
-
o-Fluorophenylalanine
-
-
o-Hydroxyphenylalanine
-
-
p-Chlorophenylalanine
-
-
p-Fluorophenylalanine
Phe
0.005 mM, 66% inhibition, competitive with prephenate
tetrathionate
-
-
trans-aconitate
-
-
Zn2+
-
0.1 mM, 58% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-3-phenylpropanol
-
activation
3-Aminotyrosine
-
activation
beta-(4-aminophenyl)-DL-alanine
-
activation
beta-(4-aminophenyl)-DL-serine
-
activation
beta-(4-fluorophenyl)-DL-alaine
-
activation
beta-phenyl-DL-serine
-
activation
bovine serum albumin
-
activation
-
D-tyrosine
DL-tyrosine
-
activation
L-isoleucine
L-leucine
L-methionine
L-Phe
-
allosteric activator, activation above 0.1 mM
L-Trp
-
allosteric activator, activation above 0.1 mM
L-tryptophan
L-Tyr
-
allosteric activator, activation above 0.1 mM
L-tyrosine
methyl L-phenylalaninate
-
activation
N-acetyl-L-Phe
-
activation
p-aminophenylalanine
-
activation
Tyr
1 mM, 70% increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.17
arogenate
1.3 - 4.88
phenylpyruvate
0.01 - 4.88
prephenate
additional information
additional information
-
Km for chorismate of wild-type and mutants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 2962
prephenate
additional information
additional information
Escherichia coli
-
kcat for chorismate of wild-type and mutants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
prephenate
Archaeoglobus fulgidus
O30012
77C, pH not specified in the publication
353
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 670
L-phenylalanine
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
L-phenylalanine
Oryza sativa
A8CF65, Q6Z3Y3
wild-type, rice PDT is a bifunctional enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.32
-
mutant F185Y, pH 7.5, 30C
0.39
-
mutant T183S, pH 7.5, 30C
2.37
-
mutant S99A, pH 7.5, 30C
4.31
-
mutant R184L, pH 7.5, 30C
6.66
-
mutant S99M, pH 7.5, 30C
6.88
-
mutant S99C, pH 7.5, 30C
7.59
-
mutant S99T, pH 7.5, 30C
8.1
-
mutant E164D, pH 7.5, 30C
9.48
-
wild-type enzyme, pH 7.5, 30C
18.2
-
crude native cell extract
37.6
-
purified recombinant prephenate dehydratase domain
40.4
-
purified recombinant mutant E159A
42.9
-
purified recombinant mutant E232A
56.9
-
purified recombinant double mutant E159A/E232A
3100
strain WSH-Z06 (pAP-B)
18000
strain WSH-Z06 (pAP-B03)
18600
strain WSH-Z06 (pAP-B01)
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.6
-
-
6.8
-
potassium phosphate buffer
7
-
,Tris-maleate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77
assay at; spectrophotometric assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
wild-type, and transformed callus lines expressing mtr1-D mutation, experimental system for feeding experiments with external L-phenylalanine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
; targeting sequence, in vitro import assay
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Paenarthrobacter aurescens (strain TC1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12200
-
ultracentrifugation
18000
-
4 * 18000, bifunctional enzyme prephenate dehydratase-arogenate dehydratase, SDS-PAGE
28300
-
2 * 28300, SDS-PAGE; 8 * 28300, SDS-PAGE
31000
x * 31000, SDS-PAGE
31413
-
x * 31413, ESI mass spectrometry
31415
-
x * 31415, calculated from sequence
32288
-
4 * 32288, calculation from nucleotide sequence
34000
-
4 * 34000, SDS-PAGE
39000
-
x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE
43100
x * 43100, SDS-PAGE
43111
-
2 * 43111, smallest native species of enzyme, calculation from nucleotide sequence; 8 * 43111, calculation from nucleotide sequence
45600
-
gel filtration
66000
trifunctional enzyme, SDS-PAGE
70946
6 * 70946, calculated from sequence
70950
calculated by sequence
73000
-
bifunctional enzyme, prephenate dehydratase-arogenate dehydratase, gel filtration
85000
-
major component, 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
125000
predicted by dynamic light scattering
134500
predicted as a tetrameric globular particle
135000
-
gel filtration
137000
-
minor component, gel filtration
144000
-
ultracentrifugation
150000
-
gel filtration
175000
-
bifunctional enzyme, chorismate mutase:prephenate dehydratase, presence of L-Phe, gel filtration
187000
-
gel filtration
210000
-
presence of activating molecules, gel filtration
420000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
homotetramer
monomer
-
1 * 35000, inactive enzyme in absence of activating molecules
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of prephenate dehydratase in a tense (T) state
-
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
-
crystal structures of prephenate dehydratase in a relaxed (R) state
-
hanging drop vapor diffusion method, using 15% (w/v) polyethylene glycol 8000, 100 mM magnesium chloride, 100 mM Tris-HCl, pH 7.4
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
37C, 5 min stable
33877
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 4
-
diluted enzyme stable for several hours
32
-
60 min, dissociation of 210000 MW enzyme to inactive 35000 Da units
42
-
absence of activators, 2 min, 60% loss of activity, presence of l-Phe or L-Tyr, 5-7% loss of activity
94
-
MjPDT unfolds in a two-state manner, Tm: 94C
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
-
unstable to freezing/thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 3 mg protein/ml
-
-20C, 40% v/v glycerol
-
-20C, 50 mM phosphate buffer, pH 7.4, 0.7 mg protein/ml, stable for 10 months
-
4C, 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
-
4C, 20% glycerol or presence of L-Met, L-Leu, prephenate, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme, chorismate mutase:prephenate dehydratase
bifunctional enzyme, prephenate dehydratase-arogenate 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)
-
gel filtration, recombinant protein
gel filtration, SDS-PAGE
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli, mtr1-D mutant gene, callus transformation by Agrobacterium tumefaciens
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
-
expressed in Escherichia coli (DE3)-RIL, pIS85 expression plasmid; overexpressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3), pET-23a(+) expression vector
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
-
gene pheA, overproduced in Escherichia coli
-
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
-
pheA gene is cloned and expressed in Escherichia coli
-
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)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the presence of aryl acids does not have a large affect on the expression of the enzyme
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
-
S298I
mutant Mtr1
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
synthesis
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