Information on EC 1.3.1.43 - arogenate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.1.43
-
RECOMMENDED NAME
GeneOntology No.
arogenate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + NAD+ = L-tyrosine + NADH + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
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L-tyrosine biosynthesis III
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Metabolic pathways
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Novobiocin biosynthesis
-
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Phenylalanine, tyrosine and tryptophan biosynthesis
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tyrosine metabolism
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
64295-75-6
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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; a mutator insertion at an equivalent position in AroDH-3, the most closely related family member to AroDH-1, is associated with opaque endosperm and stunted vegetative growth phenotypes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD(P)+
L-tyrosine + NAD(P)H + CO2
show the reaction diagram
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
prephenate + NAD(P)+
?
show the reaction diagram
prephenate + NAD+
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arogenate + NAD+
L-tyrosine + NADH + CO2
show the reaction diagram
prephenate + NAD+
?
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dihydroxyphenylalanine
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slight inhibition
4-amino-L-phenylalanine
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4-hydroxybenzoate
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4-hydroxyphenylacetate
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4-hydroxyphenylpyruvate
D-tyrosine
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DL-4-hydroxyphenyllactate
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L-phenylalanine
L-tyrosine
m-Fluoro-DL-tyrosine
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phenylpyruvate
prephenate
additional information
-
no inhibition with phenyllactate and benzoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-tyrosine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.91
L-arogenate
0.01 - 0.41
NAD+
0.07 - 0.25
prephenate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
4-hydroxylphenylpyruvate
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-
0.016 - 0.26
L-tyrosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017
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ATCC 27360
0.0058
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HGH 154
3.1
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purified enzyme, substrate prephenate
8.825
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purified enzyme, substrate L-arogenate
18.8
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25500
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6 * 25500, SDS-PAGE
28100
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2 * 28100, SDS-PAGE
32000
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? * 32000, sequence determination and SDS-PAGE
33000
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2 * 33000, recombinant His-tagged protein, forms a tetramer at high protein concentration, SDS-PAGE
36000
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2 * 36000, SDS-PAGE
37700
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2 * 37700, SDS-PAGE
38400
-
2 * 38400, SDS-PAGE
61700
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gel filtration
66000
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dimer, gel filtration
66300
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gel filtration
68000
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gel filtration
69000
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gel electrophoresis after cross-linking with dimethylsuberimidate
150000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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? * 32000, sequence determination and SDS-PAGE
hexamer
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6 * 25500, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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7 days, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in absence of glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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tyrAc gene, sequence analysis, overexpression of His-tagged protein in Escherichia coli
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tyrc gene, sequence analysis, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (645 entries)
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