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Information on EC 1.3.1.12 - prephenate dehydrogenase
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EC Tree
1.3.1.12 prephenate dehydrogenaseIUBMB 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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Word Map
- 1.3.1.12
- l-tyrosine
- h-protein
- arogenate
- hyperglycinemia
-
nonketotic
- 4-hydroxyphenylpyruvate
- aminomethyltransferase
- dahp
-
3-deoxy-d-arabino-heptulosonate
-
cyclohexadienyl
- 7-phosphate
- dimethylglycine
-
tetrahydrofolate-dependent
-
glycine-cleavage
-
aminomethyl
-
folate-binding
The enzyme appears in viruses and cellular organisms
Synonyms
t-protein, prephenate dehydrogenase, hydroxyphenylpyruvate synthase, bifunctional t-protein, pdhe-1, tyra dehydrogenase, tyrap, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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)
bifunctional T-protein
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme
CM-PD
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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-
-
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hydroxyphenylpyruvate synthase
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-
-
-
PDH
TYR1
tyrA
TyrA dehydrogenase
TyrAp
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
-
complex with EC 5.4.99.5
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
-
both reactions occur at one active site
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
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complex with EC 5.4.99.5
CM-PD
-
bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities
CM-PD
-
bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities
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PDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+
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-
-
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prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH + H+
the T-protein is a bifunctional enzyme showing chorismate mutase, EC 5.4.99.5, and prephenate dehydrogenase activities at two separate active sites
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9044-92-2
-
9044-92-2
prephenate dehydrogenase
94859-19-5
hydroxyphenylpyruvate synthase: chorismate mutase-prephenate dehydrogenase bifunctional enzyme
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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 + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
the enzyme is involved in aromatic amino acid biosynthesis
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
activity with NADP+ as coenzyme is about 10% of that with NAD+, suggesting that NAD+ is likely the preferred and physiological coenzyme
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
second step in the biosynthesis of L-tyrosine
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
key active-site residues are located at the domain interface, including His200, Arg297 and Ser179, that are involved in catalysis and/or ligand binding and are highly conserved in TyrA proteins
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
key active-site residues are located at the domain interface, including His200, Arg297 and Ser179, that are involved in catalysis and/or ligand binding and are highly conserved in TyrA proteins
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553, 390555, 671431, 684595, 685716
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
mechanism, kinetic studies
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
mechanism, kinetic studies
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390529, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
mechanism, kinetic studies
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
mechanism, kinetic studies
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
calorimetric and equilibrium measurements
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
weak activity
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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very low activity
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-
?
additional information
?
-
a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview
-
-
?
additional information
?
-
-
a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview
-
-
?
additional information
?
-
a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
the enzyme is involved in aromatic amino acid biosynthesis
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
second step in the biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390529, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+