Information on EC 2.6.1.78 - aspartate-prephenate aminotransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.6.1.78
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RECOMMENDED NAME
GeneOntology No.
aspartate-prephenate aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + oxaloacetate = prephenate + L-aspartate
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine, tyrosine and tryptophan biosynthesis
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Metabolic pathways
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-
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).
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CAS REGISTRY NUMBER
COMMENTARY hide
53230-13-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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suppression of prephenate aminotransferase leads to a severe reduction in growth and strong chlorosis symptoms. Prephenate aminotransferase silenced plants exhibit extremely reduced levels of asparagine and are greatly affected in their phenylalanine metabolism and lignin deposition. Prephenate aminotransferase suppression triggers a transcriptional reprogramming in plastid nitrogen metabolism. The enzyme is essential for plant growth and development
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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
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-
-
-
?
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
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-
-
-
?
prephenate + L-aspartate
L-arogenate + oxaloacetate
show the reaction diagram
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
show the reaction diagram
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transamination, L-glutamate is about 3fold less effective than L-aspartate
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-
?
pyruvate + L-aspartate
L-alanine + oxaloacetate
show the reaction diagram
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-
-
-
?
additional information
?
-
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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
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transamination
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-
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dihydroxyphenyllactic acid
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metabolite of rosmarinic acid
additional information
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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, 30°C
0.08
prephenate
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pH 9.0, 40°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
L-aspartate
pH 8.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.34
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purified enzyme
28.2
pH 8.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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minor fraction, chromatofocussing
5.4
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major fraction, chromatofocussing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
rosmarinic acid-producing cells
Manually annotated by BRENDA team
additional information
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activity during cell cycle
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
44000
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2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
57000
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2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
220000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
tetramer
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2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.78)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)