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Literature summary extracted from

  • Trimmer, E.E.; Wanninayake, U.S.; Fitzpatrick, P.F.
    Mechanistic studies of an amine oxidase derived from D-amino acid oxidase (2017), Biochemistry, 56, 2024-2030 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.3 Y228L/R283G (R)-alpha-methylbenzylamine as neutral amine is substrate of mutant Y228L/R283G, while an active-site residue, likely Tyr224, must be uncharged for productive binding. The oxidative half-reaction is unperturbed by the mutation and with flavin oxidation preceding product release Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.3 2.9
-
 (R)-alpha-methylbenzylamine mutant Y228L/R283G, pH 8, 25°C. The kcat/Km profile exhibits a maximum at pH 10 Sus scrofa
1.4.3.3 5 20 O2 mutant Y228L/R283G, pH 8, 25°C Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.3 Sus scrofa P00371
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.3 (R)-alpha-methylbenzylamine + H2O + O2 substrate of mutant Y228L/R283G, the neutral amine is the substrate Sus scrofa alpha-methylbenzaldehyde + NH3 + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.3 DAO
-
 Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.3 88
-
 (R)-alpha-methylbenzylamine mutant Y228L/R283G, pH 8, 25°C Sus scrofa