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Information on EC 1.3.1.79 - arogenate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.3.1.79
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.79 arogenate dehydrogenase [NAD(P)+]
IUBMB Comments
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). Enzymes that can utilize both cofactors have been reported from some Proteobacteria, including Burkholderia caryophylli, Burkholderia cepacia, Pseudomonas marginata and Delftia acidovorans.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
showSynonyms
arogenate dehydrogenase, arogenate dehydrogenase isoform 2, cyclohexadienyl dehydrogenase, Spirs_1513, tyrA, TyrAc, TyrC, ZmTyrA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Spirs_1513
tyrA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NAD(P)+ = L-tyrosine + NAD(P)H + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-arogenate:NAD(P)+ oxidoreductase (decarboxylating)
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). Enzymes that can utilize both cofactors have been reported from some Proteobacteria, including Burkholderia caryophylli, Burkholderia cepacia, Pseudomonas marginata and Delftia acidovorans.
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CAS REGISTRY NUMBER
COMMENTARY
64295-75-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prephenate + NAD(P)+
p-hydroxyphenylpyruvate + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
Flavobacterium paucimobilis
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
Flavobacterium suaveolens
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + H+ + CO2
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + H+ + CO2
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
Flavobacterium paucimobilis
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
Flavobacterium suaveolens
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
prephenate + NAD(P)+
4-hydroxyphenylpyruvate + NAD(P)H + H+ + CO2
Substrates: no substrate of wild-type, reaction of EC 1.3.1.12
Products: -
Products: -
?
prephenate + NAD(P)+
4-hydroxyphenylpyruvate + NAD(P)H + H+ + CO2
Substrates: no substrate of wild-type, reaction of EC 1.3.1.12
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
Flavobacterium paucimobilis
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
Flavobacterium suaveolens
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
Substrates: i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.74
prephenate
mutant D208N, pH 7.6, temperature not specified in the publication
0.85
L-arogenate
mutant D208N, pH 7.6, temperature not specified in the publication
0.9
L-arogenate
wild-type, pH 7.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.86
prephenate
mutant D208N, pH 7.6, temperature not specified in the publication
0.45
L-arogenate
mutant D208N, pH 7.6, temperature not specified in the publication
3.44
L-arogenate
wild-type, pH 7.6, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.57
L-arogenate
mutant D208N, pH 7.6, temperature not specified in the publication
4
L-arogenate
wild-type, pH 7.6, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
TyrC has a specific activity of 1.54 IU/mg protein, while in the presence of 0.6 mM L-Tyr the specific activity was 1.34 IU/mg protein
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). E1R5M5_SEDSS
Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
251
0
27869
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D208N
D208N
mutation introduces prephenate dehydrogenase activity
D208N
-
mutation introduces prephenate dehydrogenase activity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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
Agromyces mediolanus, Empedobacter brevis, Flavobacterium aquatile, Flavobacterium paucimobilis, Flavobacterium suaveolens, Myroides odoratus, Novosphingobium capsulatum, Sphingomonas paucimobilis, [Flavobacterium] lutescens
brenda
Keller, B.; Keller, E.; Salcher, O.; Lingens, F.
Arogenate (pretyrosine) pathway of tyrosine and phenylalanine biosynthesis in Pseudomonas aureofaciens ATCC 15926
J. Gen. Microbiol.
128
1199-1202
1982
Pseudomonas chlororaphis subsp. aureofaciens
brenda
Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis
Appl. Environ. Microbiol.
74
3284-3290
2008
Zymomonas mobilis
brenda
Zanin, L.; Zamboni, A.; Monte, R.; Tomasi, N.; Varanini, Z.; Cesco, S.; Pinton, R.
Transcriptomic analysis highlights reciprocal interactions of urea and nitrate for nitrogen acquisition by maize roots
Plant Cell Physiol.
56
532-548
2015
Zea mays (B6SS03)
brenda
Schenck, C.; Men, Y.; Maeda, H.
Conserved molecular mechanism of TyrA dehydrogenase substrate specificity underlying alternative tyrosine biosynthetic pathways in plants and microbes
Front. Mol. Biosci.
4
73
2017
Sediminispirochaeta smaragdinae (E1R5M5), Sediminispirochaeta smaragdinae DSM 11293 (E1R5M5)
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.1.79)
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