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Information on EC 4.2.1.51 - prephenate dehydratase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WIC3

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.51 prephenate dehydratase
IUBMB 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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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WIC3
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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prephenate
=
phenylpyruvate
+
H2O
+
CO2
=
+
+
Synonyms
prephenate dehydratase, chorismate mutase-prephenate dehydratase, chorismate mutase prephenate dehydratase, cm-pd, pdt protein, mtbpdt, monofunctional prephenate dehydratase, mjpdt, sa-pdt, ct-pdt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CM-PD
-
-
-
-
cyclohexydienyl dehydratase
-
-
-
-
dehydratase, prephenate
-
-
-
-
monofunctional prephenate dehydratase
-
-
-
-
P-protein
-
-
-
-
PDT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
prephenate
phenylpyruvate + H2O + CO2
show the reaction diagram
-
key regulator enzyme in L-phenylalanine biosynthesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-Phe
-
at concentration up to 0.1 mM
L-Trp
-
at concentration up to 0.1 mM
L-Tyr
-
at concentration up to 0.1 mM
NaCl
-
enzyme activity is completely abolished in the presence of 200 mM and higher concentrations of NaCl
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-Phe
-
allosteric activator, activation above 0.1 mM
L-Trp
-
allosteric activator, activation above 0.1 mM
L-Tyr
-
allosteric activator, activation above 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
prephenate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
encoded by pheA gene (Rv3838c); H37Rv
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
predicted by dynamic light scattering
134500
predicted as a tetrameric globular particle
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
determined by small angle X-ray scattering and analytical ultracentrifugation
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant protein
catalytic and regulatory domains of prephenate dehydratase, individually cloned in the NdeI/XhoI sites of pET23a vector and expressed in Escherichia coli BL21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3), pET-23a(+) expression vector
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)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team