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Literature summary extracted from

  • Negri, A.; Massey, V.; Williams, C.H.; Schopfer, L.M.
    The kinetic mechanism of beef kidney D-aspartate oxidase (1988), J. Biol. Chem., 263, 13557-13563.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.1 0.46
-
 O2 at 25°C Bos taurus
1.4.3.1 1.6
-
 D-Aspartate at 25°C Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.1 39000
-
 1 * 39000, SDS-PAGE Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.1 D-aspartate + H2O + O2 Bos taurus
-
 oxaloacetate + NH3 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.1 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.1 kidney
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.1 D-aspartate + H2O + O2
-
 Bos taurus oxaloacetate + NH3 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.1 monomer 1 * 39000, SDS-PAGE Bos taurus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.1 0.183
-
 D-Aspartate
-
 Bos taurus
1.4.3.1 0.725
-
 D-Aspartate 50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 25°C Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.1 FAD 1 mol flavin per mol protein Bos taurus