We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.3.1.13 - prephenate dehydrogenase (NADP+) for references in articles please use BRENDA:EC1.3.1.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase
-
-
-
-
prephenate dehydrogenase
-
-
-
-
prephenate-pretyrosine dehydrogenase
-
single multifunctional protein catalyzes both dehydrogenase reactions
PDH1
-
-
tyrA
-
TyrAp
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oxidative decarboxylation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
prephenate:NADP+ oxidoreductase (decarboxylating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
-
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
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
Lyngbya sp.
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
-
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
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
Lyngbya sp.
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+
-
NADP+
-
NAD+ is ineffective in replacing NADP+
NADP+
-
uses either cofactor, NADP+ and NAD+
NADP+
Pseudomonas alkanolytica
-
utilizes only NADP+
NADP+
-
absolute requirement for NADP+ as cofactor
NADP+
Lyngbya sp.
-
absolute requirement for NADP+ as cofactor
NADP+
-
absolute requirement for NADP+ as cofactor
NADP+
-
absolute requirement for NADP+ as cofactor
NADP+
-
absolute requirement for NADP+ as cofactor
NADP+
-
dual cofactor specificity with a preference for NADP+
NADP+
-
the enzyme prefers NADP+ over NAD+
NADP+
-
the enzyme prefers NADP+ over NAD+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-chloromercuriphenylsulfonic acid
-
-
p-hydroxymercurybenzoic acid
-
-
L-tyrosine
-
competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
L-tyrosine
-
competitive inhibition
additional information
-
not inhibited by L-Tyr
-
additional information
not inhibited by L-Tyr
-
additional information
-
not inhibited by L-Tyr
-
additional information
-
not inhibited by L-Tyr
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.561
NAD+
-
at pH 8.0 and 80°C
3.3
NAD+
-
at pH 8.0 and 80°C
0.005
NADP+
-
-
0.012
NADP+
-
pretyrosine as substrate
0.014
NADP+
-
prephenate as substrate
0.062
NADP+
-
at pH 8.0 and 80°C
0.36
NADP+
-
at pH 8.0 and 80°C
0.033
prephenate
-
-
0.127
prephenate
-
at 37°C, pH not specified in the publication
0.223
prephenate
-
at 37°C, pH not specified in the publication
0.319
prephenate
-
at pH 8.0 and 80°C
0.319
prephenate
-
with NAD+ as cosubstrate, at pH 8.0 and 80°C
0.443
prephenate
-
with NADP+ as cosubstrate, at pH 8.0 and 80°C
0.69
prephenate
-
with NAD+ as cosubstrate, at pH 8.0 and 80°C
0.73
prephenate
-
with NADP+ as cosubstrate, at pH 8.0 and 80°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15
prephenate
-
at pH 8.0 and 80°C
21.8
prephenate
-
at 37°C, pH not specified in the publication
26.3
prephenate
-
at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
47
prephenate
-
at pH 8.0 and 80°C
100
prephenate
-
at 37°C, pH not specified in the publication
217
prephenate
-
at 37°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.009
L-tyrosine
-
competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.5
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
90
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATCC 14987; ATCC 23055
-
-
brenda
ATCC 15309
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain ATCC 27893, 27898, 29151 and 29413
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain ATCC 29538
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
Lyngbya sp.
strain ATCC 29119, 29121 and 29126
-
-
brenda
-
-
-
brenda
-
-
-
brenda
no activity in Anabaena sp.
strains ATCC 27892, 27899, 29211 and 29414
-
-
brenda
no activity in Arabidopsis thaliana
-
-
-
brenda
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
no activity in Nostoc sp.
strain ATCC 29411 and 29132
-
-
brenda
no activity in Oryza sativa
rice
-
-
brenda
no activity in Pisum sativum
pea
-
-
brenda
no activity in Scytonema sp.
-
-
-
brenda
no activity in Scytonema sp. 29171
-
-
-
brenda
no activity in Synechocystis sp.
strain ATCC 29108
-
-
brenda
no activity in Triticum aestivum
wheat
-
-
brenda
strain ATCC 29105 and 29133
-
-
brenda
scarlet runner bean, L.
-
-
brenda
wax bean, L. var.Bountiful
-
-
brenda
Pseudomonas alkanolytica
-
-
-
brenda
strain ATCC 29404, Agmenellum quadruplicatum BG1, strain 27144, 27146 and 27192
-
-
brenda
strain ATCC 29109,27178 and 29235
-
-
brenda
broad bean, L. var. Windsor
-
-
brenda
mung bean, [L.] Wilczek, originally classified as Phaseolus aureus [L.] Roxb.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
71000
-
analytical ultracentrifugation
85000
-
analytical ultracentrifugation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 40612, calculated from amino acid sequence
homodimer
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7 - 8
-
maximum stability in this range at 22°C
390556
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
55
-
up to 10 min inactivates the enzyme
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ni-NTA column chromatography
-
Ni-NTA column chromatography, and Superdex 200 gel filtration
strain 23055, partially
-
Ni-NTA column chromatography, and Superdex 200 gel filtration
-
Ni-NTA column chromatography, and Superdex 200 gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
html completed