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Information on EC 1.3.1.13 - prephenate dehydrogenase (NADP+)
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1.3.1.13 prephenate dehydrogenase (NADP+)Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
CM-PD, PD-CM-PDT, PDH1, PRDH, prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase, prephenate dehydrogenase, prephenate-pretyrosine dehydrogenase, tyrA, TyrAp, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CM-PD
bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities
PD-CM-PDT
-
trifunctional enzyme with chorismate mutase, prephenate dehydrogenase and prephenate dehydratase activities
PDH1
PRDH
-
-
-
-
prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase
-
-
-
-
prephenate dehydrogenase
-
-
-
-
prephenate-pretyrosine dehydrogenase
-
single multifunctional protein catalyzes both dehydrogenase reactions
tyrA
TyrAp
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
prephenate:NADP+ oxidoreductase (decarboxylating)
-
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CAS REGISTRY NUMBER
COMMENTARY
37251-11-9
-
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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 + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
dual cofactor specificity with a preference for NADP+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
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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 + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
dual cofactor specificity with a preference for NADP+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-tyrosine
-
competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
L-tyrosine
-
competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Beta vulgaris subsp. vulgaris
red beet, Beta vulgaris ssp. var. conditiva, Beta vulgaris ssp. vulgaris var. rubra
-
-
brenda
no activity in Calothrix sp.
strain ATCC 27901, 27905, 29112, 29156, 29158and 29171
-
-
brenda
strain ATCC 29404, Agmenellum quadruplicatum BG1, strain 27144, 27146 and 27192
-
-
brenda
mung bean, [L.] Wilczek, originally classified as Phaseolus aureus [L.] Roxb.
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (702 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 95
80 - 95
-
the enzyme retains full dehydrogenase activity after 50 h incubation at 80°C and greater than 50% of specific activity after 50 h at 95°C
80 - 95
-
the enzyme retains full dehydrogenase activity after 50 h incubation at 80°C and greater than 50% of specific activity after 50 h at 95°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Flavobacterium sp.
brenda
Gamborg, O.L.; Keeley, F.W.
Aromatic metabolism in plants I. A study of the prephenate dehydrogenase from bean plants
Biochim. Biophys. Acta
115
65-72
1966
Klebsiella aerogenes, no activity in Beta vulgaris subsp. vulgaris, no activity in Oryza sativa, no activity in Pisum sativum, no activity in Triticum aestivum, Phaseolus coccineus, Phaseolus vulgaris, Vicia faba, Vigna radiata
brenda
Rubin, J.L.; Jensen, R.A.
Enzymology of L-tyrosine biosynthesis in mung bean (Vigna radiata [L.] Wilczek)
Plant Physiol.
64
727-734
1979
Burkholderia cepacia, Comamonas testosteroni, Pseudomonas alkanolytica, Vigna radiata
brenda
Hall, G.C.; Flick, M.B.; Gherna, R.L.; Jensen, R.A.
Biochemical diversity for biosynthesis of aromatic amino acids among the cyanobacteria
J. Bacteriol.
149
65-78
1982
Anabaena sp., Fischerella sp., Lyngbya sp., no activity in Anabaena sp., no activity in Calothrix sp., no activity in Nostoc sp., no activity in Scytonema sp. 29171, no activity in Scytonema sp., no activity in Synechocystis sp., Nostoc sp., Synechococcus sp., Synechocystis sp.
brenda
Byng, G.S.; Berry, A.; Jensen, R.A.
Evolutionary implications of features of aromatic amino acid biosynthesis in the genus Acinetobacter
Arch. Microbiol.
143
122-129
1985
Acinetobacter calcoaceticus, Acinetobacter lwoffii, Acinetobacter sp., Acinetobacter sp. C1W
brenda
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
Ignicoccus hospitalis (A8AAX2)
brenda
Shlaifer, I.; Turnbull, J.L.
Characterization of two key enzymes for aromatic amino acid biosynthesis in symbiotic archaea
Extremophiles
20
503-514
2016
Ignicoccus hospitalis (A8AAX2), Ignicoccus hospitalis, Nanoarchaeum equitans
brenda
Schenck, C.A.; Chen, S.; Siehl, D.L.; Maeda, H.A.
Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes
Nat. Chem. Biol.
11
52-57
2015
Glycine max, Medicago truncatula, no activity in Arabidopsis thaliana
brenda
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