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Information on EC 1.3.1.13 - prephenate dehydrogenase (NADP+) for references in articles please use BRENDA:EC1.3.1.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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prephenate dehydrogenase (NADP+)
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prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
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oxidative decarboxylation
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Phenylalanine, tyrosine and tryptophan biosynthesis
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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prephenate:NADP+ oxidoreductase (decarboxylating)
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CM-PD
bifunctional enzyme with chorismate mutase and prephenate dehydrogenase activities
PD-CM-PDT
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trifunctional enzyme with chorismate mutase, prephenate dehydrogenase and prephenate dehydratase activities
prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase
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prephenate dehydrogenase
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prephenate-pretyrosine dehydrogenase
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single multifunctional protein catalyzes both dehydrogenase reactions
PDH1
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tyrA
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TyrAp
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ATCC 14987; ATCC 23055
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ATCC 15309
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strain ATCC 27893, 27898, 29151 and 29413
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strain ATCC 29538
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UniProt
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Lyngbya sp.
strain ATCC 29119, 29121 and 29126
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brenda
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brenda
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brenda
no activity in Anabaena sp.
strains ATCC 27892, 27899, 29211 and 29414
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brenda
no activity in Arabidopsis thaliana
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brenda
no activity in Beta vulgaris subsp. vulgaris
red beet, Beta vulgaris ssp. var. conditiva, Beta vulgaris ssp. vulgaris var. rubra
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brenda
no activity in Calothrix sp.
strain ATCC 27901, 27905, 29112, 29156, 29158and 29171
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brenda
no activity in Nostoc sp.
strain ATCC 29411 and 29132
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brenda
no activity in Oryza sativa
rice
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brenda
no activity in Pisum sativum
pea
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brenda
no activity in Scytonema sp.
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brenda
no activity in Scytonema sp. 29171
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no activity in Synechocystis sp.
strain ATCC 29108
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no activity in Triticum aestivum
wheat
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strain ATCC 29105 and 29133
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scarlet runner bean, L.
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wax bean, L. var.Bountiful
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Pseudomonas alkanolytica
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strain ATCC 29404, Agmenellum quadruplicatum BG1, strain 27144, 27146 and 27192
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strain ATCC 29109,27178 and 29235
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broad bean, L. var. Windsor
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mung bean, [L.] Wilczek, originally classified as Phaseolus aureus [L.] Roxb.
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prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
dual cofactor specificity with a preference for NADP+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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the enzyme prefers NADP+ over NAD+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
Lyngbya sp.
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
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-
-
?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
-
the enzyme prefers NADP+ over NAD+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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-
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
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prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
A8AAX2
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-
?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NAD+
4-hydroxyphenylpyruvate + CO2 + NADH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
A8AAX2
dual cofactor specificity with a preference for NADP+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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the enzyme prefers NADP+ over NAD+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
Lyngbya sp.
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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the enzyme prefers NADP+ over NAD+
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
prephenate + NADP+
4-hydroxyphenylpyruvate + CO2 + NADPH
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?
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NAD+
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NADP+
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NAD+ is ineffective in replacing NADP+
NADP+
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uses either cofactor, NADP+ and NAD+
NADP+
Pseudomonas alkanolytica
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utilizes only NADP+
NADP+
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absolute requirement for NADP+ as cofactor
NADP+
Lyngbya sp.
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absolute requirement for NADP+ as cofactor
NADP+
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absolute requirement for NADP+ as cofactor
NADP+
-
absolute requirement for NADP+ as cofactor
NADP+
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absolute requirement for NADP+ as cofactor
NADP+
-
dual cofactor specificity with a preference for NADP+
NADP+
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the enzyme prefers NADP+ over NAD+
NADP+
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the enzyme prefers NADP+ over NAD+
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4-chloromercuriphenylsulfonic acid
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p-hydroxymercurybenzoic acid
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L-tyrosine
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competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
L-tyrosine
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competitive inhibition
additional information
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not inhibited by L-Tyr
-
additional information
not inhibited by L-Tyr
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additional information
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not inhibited by L-Tyr
-
additional information
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not inhibited by L-Tyr
-
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0.561
NAD+
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at pH 8.0 and 80°C
3.3
NAD+
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at pH 8.0 and 80°C
0.005
NADP+
-
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0.012
NADP+
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pretyrosine as substrate
0.014
NADP+
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prephenate as substrate
0.062
NADP+
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at pH 8.0 and 80°C
0.36
NADP+
-
at pH 8.0 and 80°C
0.033
prephenate
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-
0.127
prephenate
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at 37°C, pH not specified in the publication
0.223
prephenate
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at 37°C, pH not specified in the publication
0.319
prephenate
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at pH 8.0 and 80°C
0.319
prephenate
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with NAD+ as cosubstrate, at pH 8.0 and 80°C
0.443
prephenate
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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
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15
prephenate
-
at pH 8.0 and 80°C
21.8
prephenate
-
at 37°C, pH not specified in the publication
26.3
prephenate
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at 37°C, pH not specified in the publication
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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
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0.009
L-tyrosine
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competitive inhibition with respect to substrate and noncompetitively with respect to cofactor
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7.5
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90
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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71000
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analytical ultracentrifugation
85000
-
analytical ultracentrifugation
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?
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x * 40612, calculated from amino acid sequence
homodimer
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7 - 8
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maximum stability in this range at 22°C
390556
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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
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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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Ni-NTA column chromatography
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Ni-NTA column chromatography, and Superdex 200 gel filtration
strain 23055, partially
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Ni-NTA column chromatography, and Superdex 200 gel filtration
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Ni-NTA column chromatography, and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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TYR1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
431
48906
Swiss-Prot
TYR1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
452
50923
Swiss-Prot
I1MYY4_SOYBN
271
30643
TrEMBL
A0A217FAR5_ARAHY
269
30564
TrEMBL
N6WB87_9ACTO
379
39114
TrEMBL
A0A060TDP4_BLAAD
441
49779
TrEMBL
A0A084GDA5_9PEZI
456
51202
TrEMBL
F0SB67_PSESL
Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / NCIMB 13643)
417
47588
TrEMBL
F9EGL2_9ACTO
398
40155
TrEMBL
F9DZH8_STRSA
368
41132
TrEMBL
F9DNS0_9BACL
372
41108
TrEMBL
F0ILN1_STRSA
379
42337
TrEMBL
G7J2E9_MEDTR
268
30035
TrEMBL
B8M8L8_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
435
49434
TrEMBL
G4V4Q8_AMYOR
279
28344
TrEMBL
A0A2H3EIU8_9HELO
456
51416
TrEMBL
A0A091C470_9ENTE
272
31064
TrEMBL
J1SCD4_9STRE
367
40967
TrEMBL
F3UWV1_STRSA
368
41217
TrEMBL
F2C5L0_STRSA
368
41085
TrEMBL
F0I2D4_STRSA
368
41047
TrEMBL
G4CZ75_9ACTN
365
38900
TrEMBL
M5BPQ6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
309
34463
TrEMBL
A0A098BP34_9NOCA
320
32824
TrEMBL
C5P054_COCP7
Coccidioides posadasii (strain C735)
445
50378
TrEMBL
A2QD78_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
407
46115
TrEMBL
F5RMI2_9FIRM
296
31895
TrEMBL
A0A1W2TKQ9_ROSNE
432
48777
TrEMBL
F3SGQ3_STRSA
368
41067
TrEMBL
F5SLQ0_9BACL
280
30782
TrEMBL
K0KHH7_WICCF
Wickerhamomyces ciferrii (strain F-60-10 / ATCC 14091 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031)
441
49862
TrEMBL
G4CXI0_9ACTN
349
38377
TrEMBL
F3UT24_STRSA
368
41098
TrEMBL
A0A091C4J4_9ENTE
156
17999
TrEMBL
A3GGL5_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
449
50799
TrEMBL
F2BR70_STRSA
368
41019
TrEMBL
M5QXY4_9BACI
373
41797
TrEMBL
F2BBV9_9NEIS
297
31481
TrEMBL
E4RUA2_LEAB4
Leadbetterella byssophila (strain DSM 17132 / KACC 11308 / 4M15)
419
47442
TrEMBL
F2CBE0_STRSA
368
41119
TrEMBL
F3U9N7_STRSA
368
41074
TrEMBL
A0A2H3EUE3_9HELO
442
49582
TrEMBL
A0A0L1HTR8_9PLEO
375
42464
TrEMBL
I1LMW0_SOYBN
274
30910
TrEMBL
F0IVR4_STRSA
368
41005
TrEMBL
W1QHB3_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
444
49583
TrEMBL
A0A0F8DAT5_CERFI
411
45805
TrEMBL
F5SLQ1_9BACL
79
8917
TrEMBL
F0I637_STRSA
368
41074
TrEMBL
F9EV01_9NEIS
293
32346
TrEMBL
G4CIK0_9NEIS
290
31112
TrEMBL
A8AAX2_IGNH4
Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)
348
40201
TrEMBL
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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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