The Enzyme Database

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Accepted name: tryptophan 2-monooxygenase
Reaction: L-tryptophan + O2 = (indol-3-yl)acetamide + CO2 + H2O
Other name(s): tms1 (gene name); iaaM (gene name)
Systematic name: L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)
Comments: The enzyme, studied from phytopathogenic bacteria such as Pseudomonas savastanoi, is involved in a pathway for the production of (indol-3-yl)acetate (IAA), the main auxin hormone in plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-65-8
1.  Kosuge, T., Heskett, M.G. and Wilson, E.E. Microbial synthesis and degradation of indole-3-acetic acid. I. The conversion of L-tryptophan to indole-3-acetamide by an enzyme system from Pseudomonas savastanoi. J. Biol. Chem. 241 (1966) 3738–3744. [PMID: 5916389]
2.  Kuo, T.T. and Kosuge, T. Factors influencing the production and further metabolism of indole-3-acetic acid by Pseudomonas savastanoi. J. Gen. Appl. Microbiol. 15 (1969) 51–63.
3.  Hutcheson, S.W. and Kosuge, T. Regulation of 3-indoleacetic acid production in Pseudomonas syringae pv. savastanoi. Purification and properties of tryptophan 2-monooxygenase. J. Biol. Chem. 260 (1985) 6281–6287. [PMID: 3997822]
4.  Onckelen, H.V., Prinsen, E., Inze, D., Ruedeisheim, P., Lijsebettens, M.V., Follin, A., Schell, J., Montagu, M.V. and Greef, J.D. AgrobacteriumT-DNA gene1codes for tryptophan 2-monooxygenase activity in tobacco crown gall cells. FEBS Lett. 198 (1986) 357–360.
5.  Emanuele, J.J. and Fitzpatrick, P.F. Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism. Biochemistry 34 (1995) 3710–3715. [PMID: 7893667]
[EC created 1972]

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