|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
|Brevibacillus brevis S1:||tryptophan dioxygenase|
|Cupriavidus metallidurans CH34:||tryptophan dioxygenase: kynA|
|Delftia acidovorans:||tryptophan dioxygenase|
|Homo sapiens:||indoleamine 2,3-dioxygenase: INDO|
tryptophan 2,3-dioxygenase: TDO2
|Saccharomyces cerevisiae:||tryptophan 2,3-dioxygenase: BNA2|
|Streptomyces anulatus:||tryptophan 2,3-dioxygenase: acmG|
|Streptomyces parvulus:||tryptophan dioxygenase|
In Pathway: L-tryptophan degradation XI (mammalian, via kynurenine), L-tryptophan degradation I (via anthranilate), L-tryptophan degradation to 2-amino-3-carboxymuconate semialdehyde, 3-hydroxy-4-methyl-anthranilate biosynthesis
Supersedes EC numbers: 184.108.40.206, 220.127.116.11
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 18.104.22.168: tryptophan 2,3-dioxygenase
Enzyme Commission Synonyms for 22.214.171.124: 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
Enzyme Commission Primary Name for 126.96.36.199: indoleamine 2,3-dioxygenase
Enzyme Commission Synonyms for 188.8.131.52: IDO (ambiguous), tryptophan pyrrolase (ambiguous)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -89.69 [Latendresse13]
Enzyme Commission Summary for 184.108.40.206:
A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 220.127.116.11, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [Littlejohn03]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [Ren96].
Enzyme Commission Summary for 18.104.22.168:
A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 22.214.171.124, tryptophan 2,3-dioxygenase [Yamamoto67]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [Yasui86]. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [Yasui86, Littlejohn03]. Superoxide radicals can replace O2 as oxygen donor [Hirata77, Thomas99].
Dang00: Dang Y, Dale WE, Brown OR (2000). "Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway." Free Radic Biol Med 28(4);615-24. PMID: 10719243
Leeds93: Leeds JM, Brown PJ, McGeehan GM, Brown FK, Wiseman JS (1993). "Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase." J Biol Chem 268(24);17781-6. PMID: 8349662
Littlejohn03: Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ (2003). "Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase." J Biol Chem 278(32);29525-31. PMID: 12766158
Ren96: Ren S, Liu H, Licad E, Correia MA (1996). "Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme." Arch Biochem Biophys 333(1);96-102. PMID: 8806758
Uchida83: Uchida K, Shimizu T, Makino R, Sakaguchi K, Iizuka T, Ishimura Y, Nozawa T, Hatano M (1983). "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(4);2519-25. PMID: 6600455
Yasui86: Yasui H, Takai K, Yoshida R, Hayaishi O (1986). "Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients." Proc Natl Acad Sci U S A 83(17);6622-6. PMID: 2428037
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