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Literature summary for 2.6.1.1 extracted from

  • Quiroga, C.; Imperial, S.; Busquets, M.; Cortes, A.
    Comparison of some of the properties of the holoenzymes and apoenzymes of the molecular forms of chicken liver cytoplasmic aspartate aminotransferase (1991), Biochem. Soc. Trans., 19, 74S.
    View publication on PubMed
Search for more literature for 2.6.1.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.088 0.095 2-oxoglutarate pH 7.4, 30°C Gallus gallus
2.1 2.9 L-aspartate pH 7.4, 30°C Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Gallus gallus 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Gallus gallus
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
 different molecular forms: alpha, beta, gamma, delta, epsilon
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Gallus gallus oxaloacetate + L-glutamate
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Gallus gallus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
-
 Gallus gallus
60
-
 15 min, stable Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Gallus gallus
7.4 7.6
-
 Gallus gallus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Gallus gallus