tryptophan 2,3-dioxygenase;
tryptophan pyrrolase (ambiguous);
tryptophanase;
tryptophan oxygenase;
tryptamine 2,3-dioxygenase;
tryptophan peroxidase;
indoleamine 2,3-dioxygenase (ambiguous);
indolamine 2,3-dioxygenase (ambiguous);
L-tryptophan pyrrolase;
TDO;
L-tryptophan 2,3-dioxygenase

Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2;
With incorporation of two atoms of oxygen

L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)

L-tryptophan + O2 = N-formyl-L-kynurenine [RN:R00678]

R00678

L-tryptophan [CPD:C00078];
O2 [CPD:C00007]

A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [5]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [2].

1  [PMID:6600455]

Uchida K, Shimizu T, Makino R, Sakaguchi K, Iizuka T, Ishimura Y, Nozawa T, Hatano M.

Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms.

J. Biol. Chem. 258 (1983) 2519-25.

Rattus norvegicus [GN:rno], Pseudomonas acidovorans

2  [PMID:8806758]

Ren S, Liu H, Licad E, Correia MA.

Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme.

Arch. Biochem. Biophys. 333 (1996) 96-102.

Rattus norvegicus [GN:rno]

3  [PMID:8349662]

Leeds JM, Brown PJ, McGeehan GM, Brown FK, Wiseman JS.

Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase.

J. Biol. Chem. 268 (1993) 17781-6.

Rattus norvegicus [GN:rno], Pseudomonas acidovorans

4  [PMID:10719243]

Dang Y, Dale WE, Brown OR.

Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway.

Free. Radic. Biol. Med. 28 (2000) 615-24.

Rattus norvegicus [GN:rno]

5  [PMID:12766158]

Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.

Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.

J. Biol. Chem. 278 (2003) 29525-31.

Homo sapiens [GN:hsa]