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Literature summary for 2.6.1.1 extracted from

  • Reed, R.E.; Hess, J.L.
    Partial purification and characterization of aspartate aminotransferases from seedling oat leaves (1975), J. Biol. Chem., 250, 4456-4461.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Avena sativa

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast only form I occurs in chloroplast enriched fraction Avena sativa 9507
-
mitochondrion form I and II occurs in chloroplast-enriched fraction Avena sativa 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
sedimentation equilibrium centrifugation Avena sativa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Avena sativa
-
2 isozymes
-
Avena sativa
-
var. Lodi
-

Purification (Commentary)

Purification (Comment) Organism
isoenzyme I and II Avena sativa

Source Tissue

Source Tissue Comment Organism Textmining
seedling
-
Avena sativa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
120
-
-
Avena sativa

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Avena sativa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Avena sativa