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Information on EC 1.3.1.12 - prephenate dehydrogenase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30012

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EC Tree
IUBMB Comments
This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) 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, Archaea, Eukaryota
Synonyms
t-protein, prephenate dehydrogenase, hydroxyphenylpyruvate synthase, pdhe-1, bifunctional t-protein, tyra dehydrogenase, tyrap, 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)
dehydrogenase, prephenate
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hydroxyphenylpyruvate synthase
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PDH
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
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redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
prephenate:NAD+ oxidoreductase (decarboxylating)
This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
CAS REGISTRY NUMBER
COMMENTARY hide
9044-92-2
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9044-92-2
prephenate dehydrogenase
94859-19-5
hydroxyphenylpyruvate synthase: chorismate mutase-prephenate dehydrogenase bifunctional enzyme
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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 + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
the enzyme is involved in aromatic amino acid biosynthesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
activity with NADP+ as coenzyme is about 10% of that with NAD+, suggesting that NAD+ is likely the preferred and physiological coenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tyrosine
0.5 mM, 50% inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047
NAD+
pH 6.5, 87°C
0.45
prephenate
pH 6.5, 87°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
880
prephenate
pH 6,5, 87°C
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
6 * 66000, SDS-PAGE
70946
6 * 70946, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Manually annotated by BRENDA team