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Literature summary extracted from

  • Aurich, H.; Luppa, D.; Schucker, G.
    Purification and properties of l-amino acid oxidase from neurospora (1972), Acta Biol. Med. Ger., 28, 209-220.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.2 soluble
-
 Neurospora crassa
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.2 300000
-
 disc gel electrophoresis, linear acrylamide concentration Neurospora crassa

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.2 Neurospora crassa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.2
-
 Neurospora crassa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.2 culture filtrate
-
 Neurospora crassa
-
1.4.3.2 mycelium
-
 Neurospora crassa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.2 1.45
-
-
 Neurospora crassa

Storage Stability

EC Number Storage Stability Organism
1.4.3.2 4°C, purified enzyme stable for weeks Neurospora crassa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.2 L-amino acid + H2O + O2
-
 Neurospora crassa 2-oxo acid + NH3 + H2O2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.2 49
-
 L-phenylalanine Neurospora crassa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.2 9.5
-
 L-phenylalanine Neurospora crassa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.3.2 3.5 12 half maximal activity at pH 3.5 and 12 Neurospora crassa

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.2 FAD 4 mol of FAD per mol of enzyme Neurospora crassa