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Literature summary extracted from

  • Seifert, J.; Kunz, N.; Flachmann, R.; Laufer, A.; Jany, K.D.; Gassen, H.G.
    Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase (1990), Biol. Chem. Hoppe-Seyler, 371, 239-248.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.4.3.16 urea, 7 M, denaturation Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.16 iodoacetate
-
 Escherichia coli
1.4.3.16 L-aspartate substrate inactivation Escherichia coli
1.4.3.16 meso-tartrate
-
 Escherichia coli
1.4.3.16 NAD+ competitive to FAD Escherichia coli
1.4.3.16 Tetranitromethane
-
 Escherichia coli
1.4.3.16 Urea
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.16 0.5
-
 L-aspartate at aspartate concentration 1-20 mM Escherichia coli
1.4.3.16 4.1
-
 L-aspartate at L-aspartate concentration 0.2-1 mM Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.16 60000
-
 1 * 60000, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.16 L-aspartate + H2O + O2 Escherichia coli first enzyme of quinolinate synthetase system oxaloacetate + NH3 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.16 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.16
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.16 additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.16 L-aspartate + H2O + O2
-
 Escherichia coli oxaloacetate + NH3 + H2O2
-
 ?
1.4.3.16 L-aspartate + H2O + O2 first enzyme of quinolinate synthetase system Escherichia coli oxaloacetate + NH3 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.16 monomer 1 * 60000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.16 40
-
 at pH 8.0 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.16 0.0333
-
 L-aspartate
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.16 FAD flavoprotein Escherichia coli
1.4.3.16 FAD 1 mol of FAD covalently bound per mol of enzyme Escherichia coli