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Literature summary for 1.4.3.2 extracted from

  • Hanane-Fadila, Z.M.; Fatima, L.D.
    Purification, characterization and antibacterial activity of L-amino acid oxidase from Cerastes cerastes (2014), J. Biochem. Mol. Toxicol., 28, 347-354 .
    View publication on PubMed
Search for more literature for 1.4.3.2

General Stability

General Stability Organism
freezing and thawing do not act on the enzyme activity Cerastes cerastes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 L-Leu at pH 8.0 and 20°C Cerastes cerastes

Organism

Organism UniProt Comment Textmining
Cerastes cerastes
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Cerastes cerastes
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Leu + H2O + O2
-
 Cerastes cerastes 2-oxo-4-methylvaleric acid + NH3 + H2O2
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 60000, SDS-PAGE Cerastes cerastes
homodimer 2 * 56000, calculated from amino acid sequence Cerastes cerastes

Synonyms

Synonyms Comment Organism
L-amino acid: O2 oxidoreductase
-
 Cerastes cerastes
LAAO
-
 Cerastes cerastes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
-
 Cerastes cerastes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Cerastes cerastes

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Cerastes cerastes

General Information

General Information Comment Organism
physiological function the enzyme presents antibacterial activity against Staphylococcus aureus, methicillin-resistant Staphylococcus aureus, and Pseudomonas aeruginosa Cerastes cerastes