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L-arogenate + NAD+
L-tyrosine + NADH + CO2
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH + H+
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + H+ + CO2
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
prephenate + NADP+
4-hydroxyphenylpyruvate + NADPH + CO2
-
-
-
-
?
additional information
?
-
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 -
-
?
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
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
biosynthesis of L-tyrosine
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + NADH + CO2
-
-
-
-
?
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
-
very low activity
-
-
?
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
-
-
?
additional information
?
-
no activity with arogenate
-
-
?
additional information
?
-
-
no activity with arogenate
-
-
?
additional information
?
-
-
no activity with arogenate
-
-
?
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Alzheimer Disease
Diagnosis of Alzheimer's disease.
Carcinoma
Significant overexpression of the Merkel cell polyomavirus (MCPyV) large T antigen in Merkel cell carcinoma.
Carcinoma, Merkel Cell
Significant overexpression of the Merkel cell polyomavirus (MCPyV) large T antigen in Merkel cell carcinoma.
Chordoma
Emerging Therapeutic Targets in Chordomas: A Review of the Literature in the Genomic Era.
glycine dehydrogenase (aminomethyl-transferring) deficiency
Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
A missense mutation (His42Arg) in the T-protein gene from a large Israeli-Arab kindred with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: Implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism.
Hyperglycinemia, Nonketotic
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia.
Hyperglycinemia, Nonketotic
Identification of the first reported splice site mutation (IVS7-1G-->A) in the aminomethyltransferase (T-protein) gene (AMT) of the glycine cleavage complex in 3 unrelated families with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Ketogenic diet in early myoclonic encephalopathy due to non ketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH).
Hyperglycinemia, Nonketotic
Nonketotic hyperglycinemia: two patients with primary defects of P-protein and T-protein, respectively, in the glycine cleavage system.
Hyperglycinemia, Nonketotic
Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH).
Infections
Streptococcal impetigo and acute glomerulonephritis in children in Cairo.
Malaria
Plasmodium berghei glycine cleavage system T-protein is non-essential for parasite survival in vertebrate and invertebrate hosts.
Neoplasms
Expression of 15-lipoxygenase-1 in Merkel cell carcinoma is linked to advanced disease.
Neoplasms
Immortalization of neuro-endocrine cells from adrenal tumors arising in SV40 T-transgenic mice.
prephenate dehydrogenase deficiency
A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia.
prephenate dehydrogenase deficiency
Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia.
prephenate dehydrogenase deficiency
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH).
Scarlet Fever
[Serotype distribution and antimicrobial susceptibility of group A streptococci (Streptococcus pyogenes) isolated in Taiwan]
Tuberculosis
Purification and characterization of a functionally active Mycobacterium tuberculosis prephenate dehydrogenase.
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Friedrich, B.; Friedrich, C.G.; Schlegel, H.G.
Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus
J. Bacteriol.
126
712-722
1976
Cupriavidus necator
brenda
Davidson, B.E.; Hudson, G.S.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli
Methods Enzymol.
142
440-450
1987
Escherichia coli
brenda
Bode, R.; Melo, C.; Birnbaum, D.
Regulation of chorismate mutase, prephenate dehydrogenase and prephenate dehydratase of Candida maltosa
J. Basic Microbiol.
25
291-298
1985
Candida maltosa
-
brenda
Friedrich, C.G.; Friedrich, B.; Schlegel, H.G.
Regulation of Chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from alcaligenes eutrophus
J. Bacteriol.
126
723-732
1976
Cupriavidus necator
brenda
Hagino, H.; Nakayama, K.
Regulatory properties of prephenate dehydrogenase and prephenate dehydratase from Corynebacterium glutamicum
Agric. Biol. Chem.
38
2367-2376
1974
Corynebacterium glutamicum
-
brenda
Speth, A.R.; Hund, H.K.; Lingens, F.
Terminal phenylalanine and tyrosine biosynthesis of Microtetraspora glauca
Biol. Chem. Hoppe-Seyler
370
591-599
1989
Microtetraspora glauca
brenda
Berry, A.; Jensen, R.A.; Hendry, A.T.
Enzymic arrangement and allosteric regulation of the aromatic amino acid pathway in Neisseria gonorrhoeae
Arch. Microbiol.
149
87-94
1987
Neisseria gonorrhoeae
brenda
Fischer, R.; Jensen, R.
Prephenate dehydrogenase (monofunctional)
Methods Enzymol.
142
503-507
1987
Cupriavidus necator, Bacillus subtilis, Xanthomonas campestris
brenda
Mannhaupt, G.; Stucka, R.; Pilz, U.; Schwarzlose, C.; Feldmann, H.
Characterization of the prephenate dehydrogenase-encoding gene, TYR1, from Saccharomyces cerevisiae
Gene
85
303-311
1989
Saccharomyces cerevisiae
brenda
Maruya, A.; O'Connor, M.J.; Backman, K.
Genetic separability of the chorismate mutase and prephenate dehydrogenase components of the Escherichia coli tyrA gene product
J. Bacteriol.
169
4852-4853
1987
Escherichia coli
brenda
Berry, A.; Ahmad, S.; Liss, A.; Jensen, R.A.
Enzymological features of aromatic amino acid biosynthesis reflect the phylogeny of mycoplasmas
J. Gen. Microbiol.
133
2147-2154
1987
Acholeplasma laidlawii, Mycoplasmopsis gallinarum, Mycoplasma iowae, Acholeplasma laidlawii JA1
brenda
Ahmad, S.; Jensen, R.A.
The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate
FEBS Lett.
216
133-139
1987
Escherichia coli, Klebsiella pneumoniae
brenda
Hund, H.K.; Keller, B.; Lingens, F.
Phenylalanine and tyrosine biosynthesis in sporeforming members of the order Actinomycetales
Z. Naturforsch. C
42
387-393
1987
no activity in Actinomycetales
-
brenda
Christopherson, R.I.; Morrison, J.F.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli: positive cooperativity with substrates and inhibitors
Biochemistry
24
1116-1121
1985
Escherichia coli
brenda
Hudson, G.S.; Wong, V.; Davidson, B.E.
Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine
Biochemistry
23
6240-6249
1984
Escherichia coli
brenda
Hermes, J.D.; Tipton, P.A.; Fisher, M.A.; O'Leary, M.H.; Morrison, J.F.; Cleland, W.W.
Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate
Biochemistry
23
6263-6275
1984
Escherichia coli
brenda
Christopherson, R.I.; Heyde, E.; Morrison, J.F.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites
Biochemistry
22
1650-1656
1983
Escherichia coli
brenda
Waldner-Sander, S.; Keller, B.; Keller, E.; Lingens, F.
Zur Biosynthese von Phenylalanin und Tyrosin bei Flavobakterien
Hoppe-Seyler's Z. Physiol. Chem.
364
1467-1473
1983
Novosphingobium capsulatum, Sphingomonas paucimobilis
brenda
Hudson, G.S.; Howlett, G.J.; Davidson, B.E.
The binding of tyrosine and NAD+ to chorismate mutase/prephenate dehydrogenase from Escherichia coli K12 and the effects of these ligands on the activity and self-association of the enzyme. Analysis in terms of a model
J. Biol. Chem.
258
3114-3120
1983
Escherichia coli
brenda
Bhosale, S.B.; Rood, J.I.; Sneddon, M.K.; Morrison, J.F.
Production of chorismate mutase-prephenate dehydrogenase by a strain of Escherichia coli carrying a multicopy, tyrA plasmid. Isolation and properties of the enzyme
Biochim. Biophys. Acta
717
6-11
1982
Escherichia coli
brenda
Sampathkumar, P.; Morrison, J.F.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Purification and properties of the bifunctional enzyme
Biochim. Biophys. Acta
702
204-211
1982
Escherichia coli
brenda
Sampathkumar, P.; Morrison, J.F.
Chorismate mutase-prephenate dehydrogenase from Escherichia coli. Kinetic mechanism of the prephenate dehydrogenase reaction
Biochim. Biophys. Acta
702
212-219
1982
Escherichia coli
brenda
Llewellyn, D.J.; Smith, G.D.
Study of chorismate mutase-prephenate dehydrogenase in crude cell extracts of Escherichia coli
Biochemistry
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Escherichia coli
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Fazel, A.M.; Jensen, R.A.
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no activity in coryneform bacteria
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Smith, G.D.; Roberts, D.V.; Daday, A.
Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and tyrosine
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Escherichia coli
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Stenmark-Cox, S.; Jensen, R.A.
Prephenate dehydrogenase from Pseudomonas aeruginosa is a regulated component of the channel-shuttle mechanism controlling tyrosine-phenylalanine synthesis
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Pseudomonas aeruginosa
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Koch, G.L.E.; Shaw, D.C.; Gibson, F.
Studies on the relationship between the active sites of chorismate mutase-prephenate dehydrogenase from Escherichia coli or Aerobacter aerogenes
Biochim. Biophys. Acta
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Escherichia coli, Klebsiella aerogenes
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Dayan, J.; Sprinson, D.B.
Determination of prephenate dehydrogenase activity
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Escherichia coli, Salmonella sp.
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Koch, G.L.E.; Shaw, D.C.; Gibson, F.
The purification and characterisation of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12
Biochim. Biophys. Acta
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1971
Escherichia coli
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Koch, G.L.E.; Shaw, D.C.; Gibson, F.
Characterisation of the subunits of chorismate mutase-prephenate dehydrogenase from Escherichia coli K12
Biochim. Biophys. Acta
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1971
Escherichia coli
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Koch, G.L.E.; Shaw, D.C.; Gibson, F.
Studies on the subunit structure of chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes
Biochim. Biophys. Acta
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1970
Klebsiella aerogenes
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Koch, G.L.E.; Shaw, D.C.; Gibson, F.
Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase
Biochim. Biophys. Acta
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1970
Klebsiella aerogenes
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Catheside, D.E.A.
Prephenate dehydrogenase from Neurospora: Feedback activation by phenylalanine
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Neurospora sp.
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Heyde, E.; Morrison, J.F.
Kinetic studies on the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes
Biochemistry
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1978
Klebsiella aerogenes
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Heyde, E.
Chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes: evidence that the two reactions occur at one active site
Biochemistry
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1979
Klebsiella aerogenes
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Hudson, G.S.; Davidson, B.E.
Nucleotide sequence and transcription of the phenylalanine and tyrosine operons of Escherichia coli K12
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Escherichia coli
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Patel, N.; Pierson, D.L.; Jensen, R.A.
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Pseudomonas aeruginosa
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Ahmad, S.; Jensen, R.A.
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Pseudomonas flexibilis
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Byng, G.S.; Berry, A.; Jensen, R.A.
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The enzymology of prephenate dehydrogenase in Bacillus subtilis
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Bacillus subtilis
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Fischer, R.S.; Bonner, C.A.; Boone, D.R.; Jensen, R.A.
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Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli
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Escherichia coli
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Christendat, D.; Turnbull, J.L.
Identifying groups Involved in the binding of prephenate to prephenate dehydrogenase from Escherichia coli
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Escherichia coli
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Kishore, N.; Holden, M.J.; Tewari, Y.B.; Goldberg, R.N.
A thermodynamic investigation of some reactions involving prephenic acid
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Pantoea agglomerans
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Partial inactivation of chorismate mutase-prephenate dehydrogenase from Escherichia coli in the presence of analogs of chorismate
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Escherichia coli
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Vincent, S.; Chen, S.; Wilson, D.B.; Ganem, B.
Probing the overlap of chorismate mutase and prephenate dehydrogenase sites in the escherichia coli T-protein: a dehydrogenase-selective inhibitor
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Escherichia coli
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Chen, S.; Vincent, S.; Wilson, D.B.; Ganem, B.
Mapping of chorismate mutase and prephenate dehydrogenase domains in the Escherichia coli T-protein
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Escherichia coli
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Luetke-Eversloh, T.; Stephanopoulos, G.
Feedback inhibition of chorismate mutase/prephenate dehydrogenase (TyrA) of Escherichia coli: generation and characterization of tyrosine-insensitive mutants
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Escherichia coli, Escherichia coli K-12 MG1655
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Sun, W.; Singh, S.; Zhang, R.; Turnbull, J.L.; Christendat, D.
Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism
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Aquifex aeolicus
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Xu, S.; Yang, Y.; Jin, R.; Zhang, M.; Wang, H.
Purification and characterization of a functionally active Mycobacterium tuberculosis prephenate dehydrogenase
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2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Bonvin, J.; Aponte, R.A.; Marcantonio, M.; Singh, S.; Christendat, D.; Turnbull, J.L.
Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus
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Aquifex aeolicus
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Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
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74
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Zymomonas mobilis
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Olson, M.M.; Templeton, L.J.; Suh, W.; Youderian, P.; Sariaslani, F.S.; Gatenby, A.A.; Van Dyk, T.K.
Production of tyrosine from sucrose or glucose achieved by rapid genetic changes to phenylalanine-producing Escherichia coli strains
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Escherichia coli
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Patnaik, R.; Zolandz, R.R.; Green, D.A.; Kraynie, D.F.
L-tyrosine production by recombinant Escherichia coli: fermentation optimization and recovery
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Escherichia coli
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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
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Archaeoglobus fulgidus (O30012), Archaeoglobus fulgidus
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Sun, W.; Shahinas, D.; Bonvin, J.; Hou, W.; Kimber, M.S.; Turnbull, J.; Christendat, D.
The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition
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Aquifex aeolicus (O67636), Aquifex aeolicus
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Chiu, H.J.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Clayton, T.; Das, D.; Deller, M.C.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, A.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Kumar, A.; Marciano, D.; McMullan, D.; Miller, M.D.; Morse, A.T.
The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes
Acta Crystallogr. Sect. F
66
1317-1325
2010
Haemophilus influenzae (P43902), Haemophilus influenzae, Haemophilus influenzae KW20 (P43902)
brenda
Jiang, C.; Yin, B.; Tang, M.; Zhao, G.; He, J.; Shen, P.; Wu, B.
Identification of a metagenome-derived prephenate dehydrogenase gene from an alkaline-polluted soil microorganism
Antonie van Leeuwenhoek
103
1209-1219
2013
uncultured bacterium (J9XQS6)
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Ku, H.K.; Do, N.H.; Song, J.S.; Choi, S.; Yeon, S.H.; Shin, M.H.; Kim, K.J.; Park, S.R.; Park, I.Y.; Kim, S.K.; Lee, S.J.
Crystal structure of prephenate dehydrogenase from Streptococcus mutans
Int. J. Biol. Macromol.
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761-766
2011
Streptococcus mutans (Q8DUW0), Streptococcus mutans, Streptococcus mutans ATCC 700610 (Q8DUW0)
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Ku, H.; Park, S.; Yang, I.; Kim, S.
Expression and functional characterization of prephenate dehydrogenase from Streptococcus mutans
Process Biochem.
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607-612
2010
Streptococcus mutans (Q8DUW0), Streptococcus mutans ATCC 700610 (Q8DUW0)
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Shlaifer, I.; Quashie, P.K.; Kim, H.Y.; Turnbull, J.L.
Biochemical characterization of TyrA enzymes from Ignicoccus hospitalis and Haemophilus influenzae: A comparative study of the bifunctional and monofunctional dehydrogenase forms
Biochim. Biophys. Acta
1865
312-320
2017
Haemophilus influenzae, Haemophilus influenzae RD KW20
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Lopez-Nieves, S.; Pringle, A.; Hiroshi, A.M.
Biochemical characterization of TyrA dehydrogenases from Saccharomyces cerevisiae (Ascomycota) and Pleurotus ostreatus (Basidiomycota)
Arch. Biochem. Biophys.
665
12-19
2019
Saccharomyces cerevisiae, Pleurotus ostreatus (A0A386QX79), Pleurotus ostreatus
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Jones, D.D.; Horne, H.J.; Reche, P.A.; Perham, R.N.
Structural determinants of post-translational modification and catalytic specificity for the lipoyl domains of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
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Escherichia coli (P06959)
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Shabalin, I.G.; Gritsunov, A.; Hou, J.; S?awek, J.; Miks, C.D.; Cooper, D.R.; Minor, W.; Christendat, D.
Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain
FEBS J.
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2020
Bacillus anthracis (Q81P63)
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