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2-oxoglutarate + L-aspartate
L-glutamate + oxaloacetate
-
-
-
-
r
2-oxoglutarate + L-glutamate
L-glutamate + 2-oxoglutarate
-
-
-
-
r
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
L-arogenate + 2-oxoglutarate
L-glutamate + prephenate
L-arogenate + 2-oxoglutarate
prephenate + L-glutamate
-
-
-
r
L-glutamate + prephenate
L-arogenate + 2-oxoglutarate
oxaloacetate + L-aspartate
L-aspartate + oxaloacetate
-
-
-
-
r
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
prephenate + L-aspartate
L-arogenate + oxaloacetate
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
additional information
?
-
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
Lemna sp.
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
Magnolia sp.
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
about 10% of the activity with prephenate
-
-
r
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
Sorghum bicolor x Sorghum sudanesis
-
10% of the activity with prephenate at 1.0 mM substrate concentration
-
-
r
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
Sorghum sp.
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
-
-
-
?
4-hydroxyphenylpyruvate + L-glutamate
L-tyrosine + 2-oxoglutarate
-
-
-
-
?
L-arogenate + 2-oxoglutarate
L-glutamate + prephenate
-
-
-
r
L-arogenate + 2-oxoglutarate
L-glutamate + prephenate
-
-
-
r
L-glutamate + prephenate
L-arogenate + 2-oxoglutarate
-
-
-
r
L-glutamate + prephenate
L-arogenate + 2-oxoglutarate
-
-
-
r
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
-
-
-
-
r
oxaloacetate + L-glutamate
L-aspartate + 2-oxoglutarate
Sorghum bicolor x Sorghum sudanesis
-
78% of the activity with prephenate at 1.0 mM substrate concentration
-
-
r
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
Lemna sp.
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
Magnolia sp.
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
about 5% of the activity with prephenate
-
-
r
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
Sorghum sp.
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
?
phenylpyruvate + L-glutamate
L-phenylalanine + 2-oxoglutarate
-
-
-
-
?
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
-
-
-
r
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
about 50% of the activity with L-glutamate
-
-
r
prephenate + L-aspartate
L-arogenate + oxaloacetate
Sorghum bicolor x Sorghum sudanesis
-
20% of the activity with L-glutamate
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Lemna sp.
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Lemna sp.
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Magnolia sp.
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Magnolia sp.
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
important step in biosynthesis of L-tyrosine and L-phenylalanine
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
optimal prephenate concentration is 0.5-1.0 mM
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
prephenate is the preferred substrate, optimal at low concentrations of about 1 mM
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
?
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Sorghum bicolor x Sorghum sudanesis
-
important step in biosynthesis of L-tyrosine and L-phenylalanine
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Sorghum bicolor x Sorghum sudanesis
-
enzyme shows high affinity and specificity for prephenate, similar reaction rate in both reaction directions
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Sorghum sp.
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
Sorghum sp.
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
?
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
?
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
?
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
-
-
-
r
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
prephenate is the preferred substrate
L-arogenate is cyclohexadienylic acid
-
r
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
-
-
-
?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
-
-
-
?
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
-
-
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
-
about 20% of the activity with prephenate
-
-
r
pyruvate + L-glutamate
L-alanine + 2-oxoglutarate
Sorghum bicolor x Sorghum sudanesis
-
10% of the activity with prephenate at 1.0 mM substrate concentration
-
-
r
additional information
?
-
no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate
-
-
?
additional information
?
-
-
the substrate specificity of the enzyme in bacteria is less high than in plants
-
-
?
additional information
?
-
-
no activity with oxaloacetate, 2-ketoglutarate, or pyruvate with L-glutamate
-
-
?
additional information
?
-
-
substrate specificity, no activity with 4-hydroxyphenylpyruvate, phenylpyruvate, and indolepyruvate using cosubstrate L-glutamate, no activity with 4-hydroxyphenylpyruvate, phenylpyruvate, and pyruvate using cosubstrate L-aspartate
-
-
?
additional information
?
-
-
the substrate specificity of the enzyme in bacteria is less high than in plants
-
-
?
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Bonner, C.A.; Jensen, R.A.
Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris
Arch. Biochem. Biophys.
238
237-246
1985
Nicotiana sylvestris
brenda
Bonner, C.; Jensen, R.
Prephenate aminotransferase
Methods Enzymol.
142
479-487
1987
Corynebacterium glutamicum, [Brevibacterium] flavum, Nicotiana sylvestris, Sorghum sp., Spinacia oleracea, Magnolia sp., Lemna sp., Hemerocallis hybrid cultivar
brenda
Siehl, D.L.; Connelly, J.A.; Conn, E.E.
Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase
Z. Naturforsch. C
41
79-86
1986
Sorghum bicolor x Sorghum sudanesis
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 (Q9SIE1)
brenda
Graindorge, M.; Giustini, C.; Kraut, A.; Moyet, L.; Curien, G.; Matringe, M.
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms
J. Biol. Chem.
289
3198-3208
2014
Synechocystis sp. (P54691), Sinorhizobium meliloti (Q02635), Streptomyces avermitilis (Q82IK5), Streptomyces avermitilis DSM 46492 (Q82IK5)
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
Giustini, C.; Graindorge, M.; Cobessi, D.; Crouzy, S.; Robin, A.; Curien, G.; Matringe, M.
Tyrosine metabolism identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase
FEBS J.
286
2118-2134
2019
Sinorhizobium meliloti (Q02635), Arabidopsis thaliana (Q9SIE1)
brenda
Holland, C.K.; Berkovich, D.A.; Kohn, M.L.; Maeda, H.; Jez, J.M.
Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis
Plant J.
94
304-314
2018
Arabidopsis thaliana (Q9SIE1)
brenda