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Literature summary for 2.6.1.79 extracted from

  • Bonner, C.A.; Jensen, R.A.
    Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris (1985), Arch. Biochem. Biophys., 238, 237-246.
    View publication on PubMed

General Stability

General Stability Organism
pyridoxal 5'-phosphate, EDTA, and glycerol stabilize, required for activity assay Nicotiana sylvestris

Inhibitors

Inhibitors Comment Organism Structure
prephenate substrate inhibition above 1 mM, antagonism by L-glutamate Nicotiana sylvestris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate + L-glutamate Nicotiana sylvestris important step in biosynthesis of L-tyrosine and L-phenylalanine L-arogenate + 2-oxoglutarate
-
r

Organism

Organism UniProt Comment Textmining
Nicotiana sylvestris
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partially by ion exchange chromatography Nicotiana sylvestris

Source Tissue

Source Tissue Comment Organism Textmining
cell culture stable cell line ANS-1 Nicotiana sylvestris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
substrate specificity Nicotiana sylvestris
0.042
-
crude enzyme extract, substrates prephenate and L-glutamate Nicotiana sylvestris
0.073
-
partially purified enzyme, substrate pyruvate and L-glutamate Nicotiana sylvestris
0.077
-
partially purified enzyme, substrate prephenate and L-aspartate Nicotiana sylvestris
0.118
-
partially purified enzyme, substrate oxaloacetate and L-aspartate Nicotiana sylvestris
0.125
-
partially purified enzyme, substrate oxaloacetate and L-glutamate Nicotiana sylvestris
0.156
-
partially purified enzyme, substrate 2-oxoglutarate and L-aspartate Nicotiana sylvestris
0.157
-
partially purified enzyme, substrate prephenate and L-glutamate Nicotiana sylvestris
0.251
-
partially purified enzyme, substrate 2-oxoglutarate and L-glutamate Nicotiana sylvestris

Storage Stability

Storage Stability Organism
in presence of pyridoxal 5'-phosphate, EDTA, glycerol, stable for at least one month Nicotiana sylvestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + L-aspartate
-
Nicotiana sylvestris L-glutamate + oxaloacetate
-
r
2-oxoglutarate + L-glutamate
-
Nicotiana sylvestris L-glutamate + 2-oxoglutarate
-
r
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 Nicotiana sylvestris ?
-
?
oxaloacetate + L-aspartate
-
Nicotiana sylvestris L-aspartate + oxaloacetate
-
r
oxaloacetate + L-glutamate
-
Nicotiana sylvestris L-aspartate + 2-oxoglutarate
-
r
prephenate + L-aspartate
-
Nicotiana sylvestris L-arogenate + oxaloacetate
-
r
prephenate + L-glutamate important step in biosynthesis of L-tyrosine and L-phenylalanine Nicotiana sylvestris L-arogenate + 2-oxoglutarate
-
r
prephenate + L-glutamate optimal prephenate concentration is 0.5-1.0 mM Nicotiana sylvestris L-arogenate + 2-oxoglutarate
-
r
pyruvate + L-glutamate
-
Nicotiana sylvestris L-alanine + 2-oxoglutarate
-
r

Synonyms

Synonyms Comment Organism
AT-C
-
Nicotiana sylvestris
prephenate aminotransferase
-
Nicotiana sylvestris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
Nicotiana sylvestris

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 70
-
Nicotiana sylvestris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
stable, at least for 17 min Nicotiana sylvestris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.25
-
-
Nicotiana sylvestris

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required, stabilizes the enzyme Nicotiana sylvestris