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Information on EC 1.3.1.12 - prephenate dehydrogenase and Organism(s) Haemophilus influenzae and UniProt Accession P43902

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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:
Haemophilus influenzae
UNIPROT: P43902
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Word Map
The taxonomic range for the selected organisms is: Haemophilus influenzae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
t-protein, prephenate dehydrogenase, hydroxyphenylpyruvate synthase, pdhe-1, bifunctional t-protein, tyrap, tyra dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CM-PD
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bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities
dehydrogenase, prephenate
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hydroxyphenylpyruvate synthase
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PDH
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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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-
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oxidation
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-
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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 + H+
show the reaction diagram
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
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-
-
-
?
additional information
?
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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 + H+
show the reaction diagram
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
show the reaction diagram
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-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tyrosine
is bound directly at the catalytic site as a competitive inhibitor
L-Tyr
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more than 75% inhibition at 0.05 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
prephenate
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at pH 7.2 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35
prephenate
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at pH 7.2 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
730
prephenate
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at pH 7.2 and 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
SDS-PAGE and gel filtration, the dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain, structure comparisons, overview
?
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x * 40612, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
prephenate dehydrogenase component of the TyrA protein from strain Rd KW20 in complex with inhibitor tyrosine and cofactor NAD+, sitting drop vapour diffusion method, 200 nl of 19.6 mg/ml protein in 20 mM HEPES pH 8.0, 200 mM NaCl, 40 mM imidazole, 1 mM TCEP are mixed with 200 nl reservoir solution containing 0.04 M potassium dihydrogen phosphate, 20.0% v/v glycerol and 16.0% w/v PEG 8000, X-ray diffrraction structure determination and analysis at 2.0 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54
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melting temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, cleavage of the tag by TEV protease
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team