Information on EC 1.3.1.12 - prephenate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.3.1.12
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RECOMMENDED NAME
GeneOntology No.
prephenate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
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-
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prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
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oxidation
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redox reaction
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reduction
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PATHWAY
KEGG Link
MetaCyc Link
3-dimethylallyl-4-hydroxybenzoate biosynthesis
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Biosynthesis of secondary metabolites
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Metabolic pathways
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Novobiocin biosynthesis
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Phenylalanine, tyrosine and tryptophan biosynthesis
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tyrosine biosynthesis I
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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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bifunctional T-protein
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bifunctional T-protein
Escherichia coli K12
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bifunctional T-protein
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chorismate mutase-prephenate dehydratase
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme
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both reactions occur at one active site; complex with EC 5.4.99.5
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
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complex with EC 5.4.99.5
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
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complex with EC 5.4.99.5
chorismate mutase-prephenate dehydrogenase bifunctional enzyme
Escherichia coli K12
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complex with EC 5.4.99.5; complex with EC 5.4.99.5
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chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme
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chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme
Escherichia coli K12
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chorismate mutase-T:prephenate dehydrogenase bifunctional enzyme
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Chorismate mutase/prephenate dehydratase
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Chorismate mutase/prephenate dehydratase
Escherichia coli K12
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CM-TyrAp
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dehydrogenase, prephenate
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hydroxyphenylpyruvate synthase
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PDH
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PDH
Escherichia coli K-12 MG1655
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pdhE-1
Soil bacterium
J9XQS6
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tyrA
Escherichia coli K-12 MG1655, Escherichia coli K12
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CAS REGISTRY NUMBER
COMMENTARY
9044-92-2
-, prephenate dehydrogenase
94859-19-5
hydroxyphenylpyruvate synthase: chorismate mutase-prephenate dehydrogenase bifunctional enzyme
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acholeplasma laidlawii JA1
JA1
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Manually annotated by BRENDA team
strain VF5
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Manually annotated by BRENDA team
basonym Alcaligenes eutrophus
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Manually annotated by BRENDA team
K12; strains B and W
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Manually annotated by BRENDA team
L-tyrosine overproducer strain
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Manually annotated by BRENDA team
strain K-12 MG1655
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Manually annotated by BRENDA team
strain K12
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Manually annotated by BRENDA team
Escherichia coli K-12 MG1655
strain K-12 MG1655
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Manually annotated by BRENDA team
Escherichia coli K12
K12
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Manually annotated by BRENDA team
Escherichia coli K12
strain K12
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Manually annotated by BRENDA team
Neurospora sp.
pt MN64
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Manually annotated by BRENDA team
no activity in Actinomycetales
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Manually annotated by BRENDA team
no activity in coryneform bacteria
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Manually annotated by BRENDA team
Soil bacterium
uncultured alkaline-polluted bacterium
UniProt
Manually annotated by BRENDA team
Streptococcus mutans ATCC 700610
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-, P43902
chorismate mutase/prephenate dehydrogenase from Haemophilus influenzae Rd KW20 is a bifunctional enzyme that catalyzes the rearrangement of chorismate to prephenate and the NAD(P)+-dependent oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate in tyrosine biosynthesis
metabolism
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chorismate mutase/prephenate dehydrogenase from Haemophilus influenzae Rd KW20 is a bifunctional enzyme that catalyzes the rearrangement of chorismate to prephenate and the NAD(P)+-dependent oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate in tyrosine biosynthesis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Adamantane 1-acetate
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Bovine serum albumin
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at low concentrations of prephenate
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Bovine serum albumin
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formation of an enzyme-albumin complex with MW of 150000
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Bovine serum albumin
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Guanidine-HCl
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activates at low concentrations, at higher concentrations concomitant loss of activity with a multi-state pathway of denaturation
L-tryptophan
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L-tryptophan analogues
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methylated or fluorinated
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phenylalanine
Neurospora sp.
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pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
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Soil bacterium
J9XQS6
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PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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proteolytic digestion of recombinant wild-type enzyme by papain, pH 6.8, 37°C
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTA1-19
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delta19PD, more sensitive to temperature effects yielding a half-life of 55 min at 95°C versus 2 h for PD
H147N
-, O67636
inactive, binds prephenate with apparent affinity similar to wild-type
H217A
-, O67636
40fold increase in Km for prephenate, no inhibition by tyrosine
R250Q
-, O67636
10fold increase in the Km for prephenate and a 20fold increase in Ki for tyrosine
S126A
-, O67636
15fold reduction in kcat, a 10fold increase in the Km value for prephenate, and a 2-fold increase in Ki for tyrosine
H131A
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme retains 10% of dehydrogenase activity and 30% mutase activity compared to the wild-type enzyme, His131 is not an essential residue whose protonation state is critical for catalysis or substrate binding
H189N
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme shows less than 0.01% the activity of wild-type mutase and dehydrogenase
H197N
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no significant dehydrogenase activity, retains nearly wild-type mutase activity and unaltered Michaelis constants for chorismate, prephenate and NAD+
K37A
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant protein poorly expressed, no detectable mutase or dehydrogenase activity, structural changes may result in its inactivity and instability
H217N
-, O67636
30fold increase in Km for prephenate, no inhibition by tyrosine
additional information
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delta19-PDH, delta25-PDH, and delta28-PDH, which produce stable and soluble proteins, delta36-PDH, delta52-PDH, and delta55-PDH are unstable
K37Q
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, mutant enzyme exhibits no mutase activity while retaining wild-type dehydrogenase activity
additional information
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feedback-inhibition-resistant mutants toward L-tyrosine, chorismate mutase activities similar to those of the wild-type, amino acid substitutions either at Tyr263 or at residues 354 to 357
R294Q
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chorismate mutase-prephenate dehydrogenase bifunctional enzyme, R294Q substitution reduces the affinity of the enzyme for prephenate, Arg294 interacts electrostatically with the ring carboxylate at C1 of prephenate
additional information
Escherichia coli K-12 MG1655
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feedback-inhibition-resistant mutants toward L-tyrosine, chorismate mutase activities similar to those of the wild-type, amino acid substitutions either at Tyr263 or at residues 354 to 357
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