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Information on EC 1.3.1.43 - arogenate dehydrogenase
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1.3.1.43 arogenate dehydrogenaseIUBMB Comments
Arogenate dehydrogenases may utilize NAD+ (EC 1.3.1.43), NADP+ (EC 1.3.1.78), or both (EC 1.3.1.79). NAD+-specific enzymes have been reported from some bacteria and plants . Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase.
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Word Map
- 1.3.1.43
- prephenate
- l-tyrosine
- dehydratase
- chorismate
- mutase
- l-phenylalanine
- 4-hydroxyphenylpyruvate
- shikimate
-
3-deoxy-d-arabino-heptulosonate
- phenylpyruvate
- 7-phosphate
- zymomonas
- dahp
- herbicola
-
5-enolpyruvylshikimate
-
mutase-prephenate
- l-tyr
-
t-proteins
The enzyme appears in viruses and cellular organisms
Synonyms
arogenate dehydrogenase, cyclohexadienyl dehydrogenase, pretyrosine dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arogenate dehydrogenase
cyclohexadienyl dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
TyrA dehydrogenase superfamily
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
TyrA dehydrogenase superfamily
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
substrate binding and inhibitory mechanism
-
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-arogenate:NAD+ 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). NAD+-specific enzymes have been reported from some bacteria [2] and plants [3]. Some enzymes also possess the activity of EC 1.3.1.12, prephenate dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
64295-75-6
-
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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
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine
-
?
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
-
-
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
?
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
?
additional information
?
-
-
activity with prephenate and L-arogenate is unseparable during purification, thus cyclohexadienyl dehydrogenase activity
-
?
additional information
?
-
-
prephenate and L-arogenate dehydrogenase activity on one single protein, termed cyclohexadienyl dehydrogenase
-
?
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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
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
L-arogenate + NAD+
L-tyrosine + NADH + CO2
-
i.e. 3-(1-carboxy-4-hydroxycyclohexa-2,5-dien-1-yl)-L-alanine, final biosynthetic step to tyrosine
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition with phenyllactate and benzoate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
L-tyrosine
-
with L-arogenate as variable substrate, competitive inhibition
0.06
L-tyrosine
-
with prephenate as variable substrate, competitive inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
-
a maize opaque endosperm mutant (mto140), which shows retarded vegetative growth, is described. The opaque phenotype co-segregates with a mutator transposon insertion in an arogenate dehydrogenase gene (zmAroDH-1). Mto140/arodh-1 seeds show a general reduction in zein storage protein accumulation and an elevated lysine phenotype typical of other opaque endosperm mutants
Show AA Sequence and Transmembrane Helices (806 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Synechocystis sp. (strain PCC 6803 / Kazusa)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
69000
-
gel electrophoresis after cross-linking with dimethylsuberimidate
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
dimer
-
2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
additional information
-
spontaneous mutant Phe r19, growth selection, reduced activity
additional information
-
spontaneous mutant tyrB2 without any activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
tyrAc gene, sequence analysis, overexpression of His-tagged protein in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Berry, A.; Jensen, R.A.; Hendry, A.T.
Enzymic arrangement and allosteric regulation of the aromatic amino acid pathway in Neisseria gonorrhoeae
Arch. Microbiol.
149
87-94
1987
Neisseria gonorrhoeae
brenda
Hund, H.K.; Keller, B.; Lingens, F.
Phenylalanine and tyrosine biosynthesis in sporeforming members of the order Actinomycetales
Z. Naturforsch. C
42
387-393
1987
Actinomadura citrea, Actinoplanes missouriensis, Actinoplanes philippinensis, Streptomyces humiferus, Actinoplanes auranticolor, Actinoplanes campanulatus, Dactylosporangium thailandense, Micromonospora echinospora, Pilimelia terevasa, Planobispora longispora, Planomonospora venezuelensis, Spirillospora albida, Streptosporangium roseum
-
brenda
Ahmad, S.; Jensen, R.A.
Evolution of the biochemical pathway for aromatic amino acid biosynthesis in Serpens flexibilis in relationship to its phylogenetic position
Arch. Microbiol.
147
8-12
1987
Pseudomonas flexibilis
-
brenda
Lingens, F.; Keller, E.; Keller, B.
Arogenate dehydrogenase from Phenylobacterium immobile
Methods Enzymol.
142
513-518
1987
Phenylobacterium immobile
-
brenda
Keller, B.; Keller, E.; Lingens, F.
Arogenate dehydrogenase from Streptomyces phaeochromogenes. Purification and properties
Biol. Chem. Hoppe-Seyler
366
1063-1066
1985
Streptomyces phaeochromogenes
brenda
Mayer, E.; Waldner-Sander, S.; Keller, B.; Keller, E.; Lingens, F.
Purification of arogenate dehydrogenase from Phenylobacterium immobile
FEBS Lett.
179
208-212
1985
Phenylobacterium immobile
brenda
Hund, H.K.; B. r, G.; Lingens, F.
Purification and properties of arogenate dehydrogenase from Actinoplanes missouriensis
Z. Naturforsch. C
44
797-801
1989
Actinoplanes missouriensis
brenda
Byng, G.; Whitaker, R.; Flick, C.; Jensen, R.A.
Enzymology of L-tyrosine biosynthesis in corn (Zea mays)
Phytochemistry
20
1289-1292
1981
Zea mays
-
brenda
Hall, G.C.; Jensen, R.A.
Enzymological basis for growth inhibition by L-phenylalanine in the cyanobacterium Synechocystis sp. 29108
J. Bacteriol.
144
1034-1042
1980
Synechocystis sp., Synechocystis sp. 29108
brenda
Fazel, A.M.; Bowen, J.R.; Jensen, R.A.
Arogenate (pretyrosine) is an obligatory intermediate of L-tyrosine biosynthesis: confirmation in a microbial mutant
Proc. Natl. Acad. Sci. USA
77
1270-1273
1980
[Brevibacterium] flavum
brenda
Xie, G.; Bonner, C.A.; Jensen, R.A.
Cyclohexadienyl dehydrogenase from Pseudomonas stutzeri exemplifies a widespread type of tyrosine-pathway dehydrogenase in the TyrA protein family
Comp. Biochem. Physiol. C
125
65-83
2000
Pseudomonas stutzeri, Pseudomonas stutzeri JM300
brenda
Xia, T.; Jensen, R.A.
A single cyclohexadienyl dehydrogenase specifies the prephenate dehydrogenase and arogenate dehydrogenase components of the dual pathways to L-tyrosine in Pseudomonas aeruginosa
J. Biol. Chem.
265
20033-20036
1990
Pseudomonas aeruginosa
brenda
Zhao, G.; Xia, T.; Ingram, L.O.; Jensen, R.A.
An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis
Eur. J. Biochem.
212
157-165
1993
Zymomonas mobilis
brenda
Holding, D.; Meeley, R.; Hazebroek, J.; Selinger, D.; Gruis, F.; Jung, R.; Larkins, B.
Identification and characterization of the maize arogenate dehydrogenase gene family
J. Exp. Bot.
61
3663-3673
2010
Zea mays
brenda
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