Information on EC 2.6.1.78 - aspartate-prephenate aminotransferase

Word Map on EC 2.6.1.78
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.78
-
RECOMMENDED NAME
GeneOntology No.
aspartate-prephenate aminotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + oxaloacetate = prephenate + L-aspartate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
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-
SYSTEMATIC NAME
IUBMB Comments
L-arogenate:oxaloacetate aminotransferase
A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate---prephenate aminotransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
53230-13-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + L-aspartate
L-glutamate + oxaloacetate
show the reaction diagram
-
-
-
-
?
4-hydroxyphenylpyruvate + L-aspartate
L-tyrosine + oxaloacetate
show the reaction diagram
-
-
-
-
?
glyoxylate + L-aspartate
glycine + oxaloacetate
show the reaction diagram
-
-
-
-
?
indolepyruvate + L-aspartate
L-tryptophan + oxaloacetate
show the reaction diagram
-
-
-
-
?
L-arogenate + oxaloacetate
prephenate + L-aspartate
show the reaction diagram
-
-
-
r
phenylpyruvate + L-aspartate
L-phenylalanine + oxaloacetate
show the reaction diagram
-
-
-
-
?
prephenate + L-aspartate
L-arogenate + oxaloacetate
show the reaction diagram
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
show the reaction diagram
-
transamination, L-glutamate is about 3fold less effective than L-aspartate
-
-
?
pyruvate + L-aspartate
L-alanine + oxaloacetate
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
prephenate + L-aspartate
L-arogenate + oxaloacetate
show the reaction diagram
-
transamination
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dihydroxyphenyllactic acid
-
metabolite of rosmarinic acid
additional information
-
enzyme shows substrate inhibition, but no feedback inhibition by L-phenylalanine and L-tyrosine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 12
L-aspartate
0.025
oxaloacetate
pH 8.0, 30C
0.08
prephenate
-
pH 9.0, 40C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
L-aspartate
Arabidopsis thaliana
Q9SIE1
pH 8.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.34
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
minor fraction, chromatofocussing
5.4
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major fraction, chromatofocussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
rosmarinic acid-producing cells
Manually annotated by BRENDA team
additional information
-
activity during cell cycle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
tetramer
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2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, purified enzyme, 50 mM Tris-HCl, pH 8.2, 5 mM 2-mercaptoethanol, 150 mM sucrose, 1 mM EDTA, stable for at least 5 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 41fold to homogeneity by anion exchange chromatography, chromatofocusing using the major active fraction with an isoelectric point of 5.4, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli