1.3.1.12: prephenate dehydrogenase
This is an abbreviated version!
For detailed information about prephenate dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.12
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1.3.1.12
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l-tyrosine
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h-protein
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arogenate
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hyperglycinemia
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nonketotic
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4-hydroxyphenylpyruvate
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aminomethyltransferase
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dahp
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3-deoxy-d-arabino-heptulosonate
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cyclohexadienyl
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7-phosphate
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dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
- 1.3.1.12
- l-tyrosine
- h-protein
- arogenate
- hyperglycinemia
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nonketotic
- 4-hydroxyphenylpyruvate
- aminomethyltransferase
- dahp
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3-deoxy-d-arabino-heptulosonate
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cyclohexadienyl
- 7-phosphate
- dimethylglycine
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tetrahydrofolate-dependent
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glycine-cleavage
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aminomethyl
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folate-binding
Reaction
Synonyms
AceF, AroQ, bifunctional T-protein, chorismate mutase-prephenate dehydratase, chorismate mutase-prephenate dehydrogenase bifunctional enzyme, chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme, Chorismate mutase/prephenate dehydratase, CM-PD, CM-TyrAp, CM/PDT/PDHG, CMPD, dehydrogenase, prephenate, hydroxyphenylpyruvate synthase, PD, PDH, pdhE-1, PDHG, T-protein, TYR1, tyrA, TyrA dehydrogenase, TyrAp
ECTree
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Substrates Products
Substrates Products on EC 1.3.1.12 - prephenate dehydrogenase
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REACTION DIAGRAM
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
the enzyme is involved in aromatic amino acid biosynthesis
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?
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
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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second step in the biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
4-hydroxyphenylpyruvate + CO2 + NADH + H+
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
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?
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+
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?
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 + NADH + CO2
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biosynthesis of L-tyrosine
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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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
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mechanism, kinetic studies
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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mechanism, kinetic studies
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ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
3557, 390516, 390518, 390521, 390522, 390524, 390526, 390527, 390528, 390529, 390530, 390532, 390537, 390538, 390539, 390540, 390546, 390552, 390553
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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-
ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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mechanism, kinetic studies
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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mechanism, kinetic studies
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ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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ir
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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-
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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calorimetric and equilibrium measurements
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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-
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
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biosynthesis of L-tyrosine
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?
4-hydroxyphenylpyruvate + NADH + H+ + CO2
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
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?
4-hydroxyphenylpyruvate + CO2 + NADPH
weak activity
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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very low activity
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?
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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?