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Literature summary for 1.13.12.3 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)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas savastanoi
-
recombinant
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Pseudomonas savastanoi

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas savastanoi