Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.1 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]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Bos taurus
-

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

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

Cofactor

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