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Literature summary for 1.4.3.2 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
Search for more literature for 1.4.3.2

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Neurospora crassa
-
-

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Neurospora crassa

Source Tissue

Source Tissue Comment Organism Textmining
culture filtrate
-
 Neurospora crassa
-
mycelium
-
 Neurospora crassa
-

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

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

Cofactor

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