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Literature summary extracted from

  • George, H.; Gabay, S.
    Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase (1968), Biochim. Biophys. Acta, 167, 555-566.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.6.1.27 2-mercaptoethanol preincubation, activates Sus scrofa
2.6.1.27 additional information no activation by: pyridoxine, pyridoxal, pyridoxamine Sus scrofa
2.6.1.27 phosphate maximal activity in presence of phosphate buffer, in absence reaction proceeds at 50% of that observed in optimal phosphate concentration Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.27 4-Fluorophenylalanine 32 mM, 50% inhibition Sus scrofa
2.6.1.27 additional information not affected by metal chelators and high concentration of ammonium sulfate; reduced activity in cacodylate, Tris and borate buffers Sus scrofa
2.6.1.27 p-chloromercuribenzoate reduced by preincubation with L-phenylalanine and pyridoxal phosphate and reversed by a subsequent preincubation with 2-mercaptoethanol Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.27 0.74
-
 2-oxoglutarate cosubstrate phenylalanine, pH 8.0, 37°C Sus scrofa
2.6.1.27 3.8
-
 L-tyrosine pH 8.0, 37°C Sus scrofa
2.6.1.27 6
-
 L-3,4-dihydroxyphenylalanine pH 8.0, 37°C Sus scrofa
2.6.1.27 7
-
 4-Fluorophenylalanine pH 8.0, 37°C Sus scrofa
2.6.1.27 15
-
 L-tryptophan pH 8.0, 37°C Sus scrofa
2.6.1.27 50
-
 L-phenylalanine pH 8.0, 37°C Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.27 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.27 about 900fold Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.27 brain cortex Sus scrofa
-
2.6.1.27 brain cortex
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.27 7.04
-
 reverse reaction, purified enzyme Sus scrofa

Storage Stability

EC Number Storage Stability Organism
2.6.1.27 -20°C, 0.40 M potassium phosphate buffer, pH 8.0, highly purified enzyme stable for at least 2 weeks Sus scrofa
2.6.1.27 -20°C, 100fold purified enzyme, 0.4 M potassium phosphate, pH 8.0, stable for at least 9 months Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.27 5-hydroxytryptophan + 2-oxoglutarate DL-5-hydroxytryptophan, 62% as effective as L-phenylalanine Sus scrofa 3-(5-hydroxyindole)-2-oxopropanoate + L-glutamate
-
 ?
2.6.1.27 DL-p-fluorophenylalanine + 2-oxoglutarate 41% as effective as phenylalanine Sus scrofa 3-(4-fluorophenyl)-2-oxopropanoate + L-glutamate
-
 ?
2.6.1.27 L-3,4-dihydroxyphenylalanine + 2-oxoglutarate 46% as effective as L-phenylalanine Sus scrofa 3-(3,4-dihydroxyphenyl)-2-oxopropanoate + L-glutamate
-
 ?
2.6.1.27 L-aspartate + phenylpyruvate 10% as effective as L-glutamate Sus scrofa 2-oxosuccinic acid + L-phenylalanine
-
 r
2.6.1.27 L-histidine + 2-oxoglutarate 35% as effective as L-phenylalanine Sus scrofa 3-(1H-imidazol-4-yl)-2-oxopropanoate + L-glutamate
-
 ?
2.6.1.27 L-phenylalanine + 2-oxoglutarate
-
 Sus scrofa L-glutamate + phenylpyruvate
-
 r
2.6.1.27 L-phenylalanine + 2-oxosuccinic acid 70% as effective as 2-oxoglutarate Sus scrofa phenylpyruvate + L-aspartate
-
 r
2.6.1.27 L-tryptophan + 2-oxoglutarate 52% of the activity with L-phenylalanine Sus scrofa L-glutamate + 3-indole-2-oxopropanoate
-
 ?
2.6.1.27 L-tyrosine + 2-oxoglutarate 49% of the activity with L-phenylalanine Sus scrofa L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
 ?
2.6.1.27 additional information substrate specificity Sus scrofa ?
-
 ?
2.6.1.27 additional information no activity with D-phenylalanine and D-glutamic acid Sus scrofa ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.27 37
-
 assay at Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.27 8
-
 assay at Sus scrofa
2.6.1.27 8 9 phenylalanine Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.27 pyridoxal 5'-phosphate pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate Sus scrofa
2.6.1.27 pyridoxamine 5'-phosphate pyridoxamine 5'-phosphate and pyridoxal phosphate are effective in partially restoring the apoenzyme activity and in stimulating the holoenzyme pyridoxamine phosphate, pyridoxamine phosphate is somewhat more effective than pyridoxal phosphate Sus scrofa