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Literature summary for 2.6.1.1 extracted from

  • Yagi, T.; Kagamiyama, H.; Nozaki, M.
    Aspartate: 2-oxoglutarate aminotransferase from bakers yeast: crystallization and characterization (1982), J. Biochem., 92, 35-43.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
2 * 45000, SDS-PAGE Saccharomyces cerevisiae
90000 92000 gel filtration, sedimentation equilibrium analysis Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
Saccharomyces cerevisiae oxaloacetate + L-glutamate
-
?
L-aspartate + 2-oxoglutarate
-
Saccharomyces cerevisiae oxaloacetate + L-glutamate
-
r
L-cysteine sulfinic acid + 2-oxoglutarate 48% of the activity with L-glutamate Saccharomyces cerevisiae 2-oxo-3-sulfinopropionic acid + L-glutamate
-
?
additional information substrate specificity Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 45000, SDS-PAGE Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate a pyridoxal 5'-phosphate protein Saccharomyces cerevisiae
pyridoxal 5'-phosphate 1.7-1.9 mol per mol of enzyme Saccharomyces cerevisiae