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Information on EC 4.2.1.51 - prephenate dehydratase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30012

for references in articles please use BRENDA:EC4.2.1.51
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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:
Archaeoglobus fulgidus
UNIPROT: O30012
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
prephenate dehydratase, chorismate mutase-prephenate dehydratase, chorismate mutase prephenate dehydratase, cm-pd, mtbpdt, pdt protein, mjpdt, monofunctional prephenate dehydratase, sa-pdt, ct-pdt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
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)
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
the enzyme is involved in aromatic amino acid biosynthesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-phenylalanine
inhibits activity at 5 microM, competitive inhibition
Phe
0.005 mM, 66% inhibition, competitive with prephenate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tyrosine
enzyme activation by 70% at 1 mM
Tyr
1 mM, 70% increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
phenylpyruvate
measuring the appearance of phenylpyruvate at 320 nm, performed with 1 mM prephenate in 200 mM Tris buffer
1.3
prephenate
77°C, pH not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
prephenate
77°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
spectrophotometric assay performed at several different pH values
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in aromatic amino acid biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
420000
gel filtration
66000
trifunctional enzyme, SDS-PAGE
70946
6 * 70946, calculated from sequence
70950
calculated by sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli (DE3)-RIL, pIS85 expression plasmid
overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team