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Literature summary for 2.6.1.79 extracted from

  • Siehl, D.L.; Connelly, J.A.; Conn, E.E.
    Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase (1986), Z. Naturforsch. C, 41, 79-86.
    View publication on PubMed
Search for more literature for 2.6.1.79

General Stability

General Stability Organism
pyridoxal 5'-phosphate, EDTA, and glycerol stabilize, required for activity assay Sorghum bicolor x Sorghum sudanesis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
 prephenate pH 8.0 Sorghum bicolor x Sorghum sudanesis
0.8
-
 L-arogenate pH 8.0 Sorghum bicolor x Sorghum sudanesis
1.07
-
 L-glutamate pH 8.0 Sorghum bicolor x Sorghum sudanesis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sorghum bicolor x Sorghum sudanesis
-
 hybrid
-

Purification (Commentary)

Purification (Comment) Organism
partially by ion exchange chromatography Sorghum bicolor x Sorghum sudanesis

Source Tissue

Source Tissue Comment Organism Textmining
shoot etiolated, 4-days-old Sorghum bicolor x Sorghum sudanesis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 partially purified enzyme, activity of prephenate aminotransferase as a function of the concentration of prephenate and glutamate Sorghum bicolor x Sorghum sudanesis
additional information
-
 substrate specificity Sorghum bicolor x Sorghum sudanesis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylpyruvate + L-glutamate 10% of the activity with prephenate at 1.0 mM substrate concentration Sorghum bicolor x Sorghum sudanesis L-tyrosine + 2-oxoglutarate
-
 r
oxaloacetate + L-glutamate 78% of the activity with prephenate at 1.0 mM substrate concentration Sorghum bicolor x Sorghum sudanesis L-aspartate + 2-oxoglutarate
-
 r
prephenate + L-aspartate 20% of the activity with L-glutamate Sorghum bicolor x Sorghum sudanesis L-arogenate + oxaloacetate
-
 r
prephenate + L-glutamate important step in biosynthesis of L-tyrosine and L-phenylalanine Sorghum bicolor x Sorghum sudanesis L-arogenate + 2-oxoglutarate
-
 r
prephenate + L-glutamate enzyme shows high affinity and specificity for prephenate, similar reaction rate in both reaction directions Sorghum bicolor x Sorghum sudanesis L-arogenate + 2-oxoglutarate
-
 r
pyruvate + L-glutamate 10% of the activity with prephenate at 1.0 mM substrate concentration Sorghum bicolor x Sorghum sudanesis L-alanine + 2-oxoglutarate
-
 r

Synonyms

Synonyms Comment Organism
prephenate aminotransferase
-
 Sorghum bicolor x Sorghum sudanesis
prephenate: glutamate aminotransferase
-
 Sorghum bicolor x Sorghum sudanesis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Sorghum bicolor x Sorghum sudanesis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 95% remaining activity after 17 min Sorghum bicolor x Sorghum sudanesis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Sorghum bicolor x Sorghum sudanesis

pH Range

pH Minimum pH Maximum Comment Organism
6 10.5 no activity below pH 6.0 and above pH 10.5 Sorghum bicolor x Sorghum sudanesis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Sorghum bicolor x Sorghum sudanesis

pI Value

Organism Comment pI Value Maximum pI Value
Sorghum bicolor x Sorghum sudanesis isoelectric focusing
-
 5.2