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Literature summary extracted from

  • Buzenet, A.M.; Fages, C.; Bloch-Tardy, M.; Gonnard, P.
    Purification and properties of 4-aminobutyrate 2-ketoglutarate aminotransferase from pig liver (1978), Biochim. Biophys. Acta, 522, 400-411.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.19 2-oxoglutarate
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.19 0.7
-
 2-oxoglutarate 37°C Sus scrofa
2.6.1.19 1.1
-
 4-aminobutanoate 37°C Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.19 55000
-
 2 * 55000, liver enzyme, SDS-PAGE Sus scrofa
2.6.1.19 105000
-
 gel filtration Sus scrofa
2.6.1.19 110000
-
 liver enzyme, gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.19 4-aminobutanoate + 2-oxoglutarate Sus scrofa key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass 4-oxobutanoate + L-glutamate
-
 ?
2.6.1.19 4-aminobutanoate + 2-oxoglutarate Sus scrofa involved in beta-alanine metabolism 4-oxobutanoate + L-glutamate
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.19 cationic (I) and anionic (II) form Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.6.1.19 liver
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.19 1.8 3.5 37°C Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.19 3-aminoisobutanoate + 2-oxoglutarate transamination at 14% the rate of 4-aminobutanoate Sus scrofa L-glutamate + 3-oxoisobutanoate
-
 r
2.6.1.19 4-aminobutanoate + 2-oxoglutarate
-
 Sus scrofa 4-oxobutanoate + L-glutamate
-
 r
2.6.1.19 4-aminobutanoate + 2-oxoglutarate key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass Sus scrofa 4-oxobutanoate + L-glutamate
-
 ?
2.6.1.19 4-aminobutanoate + 2-oxoglutarate involved in beta-alanine metabolism Sus scrofa 4-oxobutanoate + L-glutamate
-
 ?
2.6.1.19 5-aminopentanoate + 2-oxoglutarate transamination at 85% the rate of 4-aminobutanoate Sus scrofa L-glutamate + 5-oxopentanoate
-
 ?
2.6.1.19 beta-alanine + 2-oxoglutarate effective amino group donor Sus scrofa malonic semialdehyde + L-glutamate
-
 r
2.6.1.19 DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate transamination at 20% the rate of 4-aminobutanoate Sus scrofa L-glutamate + 3-hydroxy-4-oxobutanoate
-
 r
2.6.1.19 additional information overview Sus scrofa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.19 dimer 2 * 55000, liver enzyme, SDS-PAGE Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.19 additional information
-
 pI: 5.9 and 6.35 (isozyme II), pI: 6.1 and 6.3 (isozyme I) Sus scrofa
2.6.1.19 8.7
-
 isozyme II Sus scrofa
2.6.1.19 8.8
-
 isozyme I Sus scrofa