Information on EC 2.6.1.79 - glutamate-prephenate aminotransferase

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

EC NUMBER
COMMENTARY hide
2.6.1.79
-
RECOMMENDED NAME
GeneOntology No.
glutamate-prephenate aminotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-phenylalanine biosynthesis II
-
-
L-tyrosine biosynthesis II
-
-
L-tyrosine biosynthesis III
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
phenylalanine metabolism
-
-
tyrosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arogenate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate---prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1].
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
day lily
-
-
Manually annotated by BRENDA team
Lemna sp.
duckweed
-
-
Manually annotated by BRENDA team
Magnolia sp.
-
-
-
Manually annotated by BRENDA team
cf. EC 2.6.1.1
UniProt
Manually annotated by BRENDA team
Sorghum bicolor x Sorghum sudanesis
hybrid
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cf. EC 2.6.1.17
UniProt
Manually annotated by BRENDA team
cf. EC 2.6.1.17
UniProt
Manually annotated by BRENDA team
cf. EC 2.6.1.42
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
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
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
-
-
-
-
r
2-oxoglutarate + L-glutamate
L-glutamate + 2-oxoglutarate
show the reaction diagram
-
-
-
-
r
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
show the reaction diagram
L-arogenate + 2-oxoglutarate
prephenate + L-glutamate
show the reaction diagram
-
-
-
r
oxaloacetate + L-aspartate
L-aspartate + oxaloacetate
show the reaction diagram
-
-
-
-
r
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
show the reaction diagram
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
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
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
show the reaction diagram
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
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-glutamate
L-arogenate + 2-oxoglutarate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
prephenate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
2-oxoglutarate
pH 8.0, 30C
0.8
L-arogenate
Sorghum bicolor x Sorghum sudanesis
-
pH 8.0
1.07 - 5.6
L-glutamate
0.02 - 0.13
prephenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
200
L-glutamate
Arabidopsis thaliana
Q9SIE1
pH 8.0, 30C
24 - 60
prephenate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.042
-
crude enzyme extract, substrates prephenate and L-glutamate
0.073
-
partially purified enzyme, substrate pyruvate and L-glutamate
0.077
-
partially purified enzyme, substrate prephenate and L-aspartate
0.118
-
partially purified enzyme, substrate oxaloacetate and L-aspartate
0.125
-
partially purified enzyme, substrate oxaloacetate and L-glutamate
0.156
-
partially purified enzyme, substrate 2-oxoglutarate and L-aspartate
0.157
-
partially purified enzyme, substrate prephenate and L-glutamate
0.251
-
partially purified enzyme, substrate 2-oxoglutarate and L-glutamate
8.3
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
Sorghum bicolor x Sorghum sudanesis
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10.5
Sorghum bicolor x Sorghum sudanesis
-
no activity below pH 6.0 and above pH 10.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
Sorghum bicolor x Sorghum sudanesis
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Sorghum bicolor x Sorghum sudanesis
-
etiolated, 4-days-old
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
88000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate, EDTA, and glycerol stabilize, required for activity assay
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, purified enzyme is stable for at least 1 month, partially purified enzyme is stable for at least several months
-
in presence of pyridoxal 5'-phosphate, EDTA, glycerol, stable for at least one month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
252fold from cell culture by ammonium sulfate fractionation, heat treatment, affinity chromatography, and gel filtration
-
partially by ion exchange chromatography
to homogeneity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli