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Information on EC 2.6.1.78 - aspartate-prephenate aminotransferase for references in articles please use BRENDA:EC2.6.1.78
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EC Tree
IUBMB Comments A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate---prephenate aminotransferase).
The enzyme appears in viruses and cellular organisms
Synonyms
Pat, prephenate aminotransferase,
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prephenate aminotransferase
Pat
-
-
prephenate aminotransferase
-
-
prephenate aminotransferase
-
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L-arogenate + oxaloacetate = prephenate + L-aspartate
-
-
-
-
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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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2-oxoglutarate + L-aspartate
L-glutamate + oxaloacetate
-
-
-
-
?
4-hydroxyphenylpyruvate + L-aspartate
L-tyrosine + oxaloacetate
-
-
-
-
?
glyoxylate + L-aspartate
glycine + oxaloacetate
-
-
-
-
?
indolepyruvate + L-aspartate
L-tryptophan + oxaloacetate
-
-
-
-
?
L-arogenate + oxaloacetate
prephenate + L-aspartate
-
-
-
r
phenylpyruvate + L-aspartate
L-phenylalanine + oxaloacetate
-
-
-
-
?
prephenate + L-aspartate
L-arogenate + oxaloacetate
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
transamination, L-glutamate is about 3fold less effective than L-aspartate
-
-
?
pyruvate + L-aspartate
L-alanine + oxaloacetate
-
-
-
-
?
additional information
?
-
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
transamination
-
-
?
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
-
-
r
additional information
?
-
-
substrate specificity, highest activity with 2-oxoglutarate and L-aspartate as substrates, low activity with indolepyruvate and glyoxylate
-
-
-
additional information
?
-
-
no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate
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-
-
additional information
?
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no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate
-
-
-
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prephenate + L-aspartate
L-arogenate + oxaloacetate
-
transamination
-
-
?
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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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0.025
oxaloacetate
pH 8.0, 30°C
0.08
prephenate
-
pH 9.0, 40°C
0.08
L-aspartate
-
pH 9.0, 40°C
12
L-aspartate
pH 8.0, 30°C
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65
L-aspartate
pH 8.0, 30°C
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5
-
minor fraction, chromatofocussing
5.4
-
major fraction, chromatofocussing
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-
-
-
brenda
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
SwissProt
brenda
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-
-
brenda
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-
rosmarinic acid-producing cells
brenda
additional information
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activity during cell cycle
brenda
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-
brenda
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-
brenda
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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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PAT_ARATH
475
0
51000
Swiss-Prot
PAT_PETHY
479
0
51743
Swiss-Prot
A0A251S9V0_HELAN
481
0
51608
TrEMBL
A0A2I0B401_9ASPA
432
0
46761
TrEMBL
A0A2H9ZU16_9ASPA
395
0
43499
TrEMBL
A0A2G9HKC5_9LAMI
479
0
51526
TrEMBL
A0A2G9IAH1_9LAMI
476
0
51217
TrEMBL
A0A1Z5JQG7_FISSO
435
0
46744
TrEMBL
A0A2G9HKB5_9LAMI
480
0
51727
TrEMBL
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43000
x * 43000, SDS-PAGE
44000
-
2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
57000
-
2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
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tetramer
-
2 * 44000 + 2 * 57000, alpha2beta2-structure, SDS-PAGE
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-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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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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expression in Escherichia coli
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De-Eknamkul, W.; Ellis, B.E.
Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures
Arch. Biochem. Biophys.
267
87-94
1988
Anchusa officinalis
brenda
Graindorge, M.; Giustini, C.; Jacomin, A.C.; Kraut, A.; Curien, G.; Matringe, M.
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis
FEBS Lett.
584
4357-4360
2010
Arabidopsis thaliana, Arabidopsis thaliana (Q9SIE1)
brenda
de la Torre, F.; El-Azaz, J.; Avila, C.; Canovas, F.M.
Deciphering the role of aspartate and prephenate aminotransferase activities in plastid nitrogen metabolism
Plant Physiol.
164
92-104
2014
Nicotiana benthamiana
brenda
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