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Literature summary extracted from

  • Ralph, E.C.; Anderson, M.A.; Cleland, W.W.; Fitzpatrick, P.F.
    Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and (15)N kinetic isotope effects on alanine oxidation by an l-amino acid oxidase (2006), Biochemistry, 45, 15844-15852.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.12.3 L-tryptophan + O2 Pseudomonas savastanoi oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.3 Pseudomonas savastanoi
-
 recombinant
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.3 recombinant Pseudomonas savastanoi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.3 L-alanine + O2 oxidation of alanine occurs through a hydride transfer mechanism Pseudomonas savastanoi acetamide + CO2 + H2O
-
 ?
1.13.12.3 L-tryptophan + O2 oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid Pseudomonas savastanoi ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.3 FAD
-
 Pseudomonas savastanoi