|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
Enzymes and Genes:
tryptophan dioxygenase ( Streptomyces parvulus )
tryptophan dioxygenase ( Delftia acidovorans )
tryptophan dioxygenase ( Brevibacillus brevis S1 )
tryptophan dioxygenase : kynA ( Cupriavidus metallidurans CH34 )
tryptophan 2,3-dioxygenase : BNA2 ( Saccharomyces cerevisiae )
tryptophan 2,3-dioxygenase : TDO2 ( Homo sapiens )
indoleamine 2,3-dioxygenase : INDO ( Homo sapiens )
Supersedes EC numbers: 18.104.22.168, 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name for 126.96.36.199: tryptophan 2,3-dioxygenase
Enzyme Commission Synonyms for 188.8.131.52: 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 184.108.40.206: indoleamine 2,3-dioxygenase
Enzyme Commission Synonyms for 220.127.116.11: IDO (ambiguous), tryptophan pyrrolase (ambiguous)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -89.69 [Latendresse13]
Enzyme Commission Summary for 18.104.22.168:
Catalyzes, together with EC 22.214.171.124, the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism. Specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan. Formerly EC 126.96.36.199 and EC 188.8.131.52.
Enzyme Commission Summary for 184.108.40.206:
A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 220.127.116.11, 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].
Relationship Links: BRENDA:EC:18.104.22.168 , BRENDA:EC:22.214.171.124 , ENZYME:EC:126.96.36.199 , ENZYME:EC:188.8.131.52 , IUBMB-ExplorEnz:EC:184.108.40.206 , IUBMB-ExplorEnz:EC:220.127.116.11 , UniProt:RELATED-TO:P21643
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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