The Enzyme Database

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EC 1.13.11.11     
Accepted name: tryptophan 2,3-dioxygenase
Reaction: L-tryptophan + O2 = N-formyl-L-kynurenine
For diagram of tryptophan catabolism, click here
Other name(s): 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; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-51-1
References:
1.  Uchida, K., Shimizu, T., Makino, R., Sakaguchi, K., Iizuka, T., Ishimura, Y., Nozawa, T. and 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) 2519–2525. [PMID: 6600455]
2.  Ren, S., Liu, H., Licad, E. and Correia, M.A. 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. [DOI] [PMID: 8806758]
3.  Leeds, J.M., Brown, P.J., McGeehan, G.M., Brown, F.K. and Wiseman, J.S. Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase. J. Biol. Chem. 268 (1993) 17781–17786. [PMID: 8349662]
4.  Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615–624. [DOI] [PMID: 10719243]
5.  Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525–29531. [DOI] [PMID: 12766158]
[EC 1.13.11.11 created 1961 as EC 1.11.1.4, deleted 1964, reinstated 1965 as EC 1.13.1.12, transferred 1972 to EC 1.13.11.11, modified 1989, modified 2006]
 
 
EC 1.13.11.26     
Accepted name: peptide-tryptophan 2,3-dioxygenase
Reaction: [protein]-L-tryptophan + O2 = [protein]-N-formyl-L-kynurenine
Glossary: N-formyl-L-kynurenine = (2S)-2-amino-4-[2-(formamido)phenyl]-4-oxobutanoic acid
Other name(s): pyrrolooxygenase; peptidyltryptophan 2,3-dioxygenase; tryptophan pyrrolooxygenase; [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Also acts on tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-64-7
References:
1.  Frydman, R.B., Tomaro, M.L. and Frydman, B. Pyrrolooxygenase: its action on tryptophan-containing enzymes and peptides. Biochim. Biophys. Acta 284 (1972) 80–89. [DOI] [PMID: 4403729]
2.  Camoretti-Mercado, B. and Frydman, R.B. Separation of tryptophan pyrrolooxygenase into three molecular forms. A study of their substrate specificities using tryptophyl-containing peptides and proteins. Eur. J. Biochem. 156 (1986) 317–325. [DOI] [PMID: 3699018]
[EC 1.13.11.26 created 1972, modified 2011]
 
 
EC 1.13.11.52     
Accepted name: indoleamine 2,3-dioxygenase
Reaction: (1) D-tryptophan + O2 = N-formyl-D-kynurenine
(2) L-tryptophan + O2 = N-formyl-L-kynurenine
For diagram of tryptophan catabolism, click here
Other name(s): IDO (ambiguous); tryptophan pyrrolase (ambiguous); D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: D-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. 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 [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-51-1
References:
1.  Yamamoto, S. and Hayaishi, O. Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes. J. Biol. Chem. 242 (1967) 5260–5266. [PMID: 6065097]
2.  Yasui, H., Takai, K., Yoshida, R. and Hayaishi, O. Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients. Proc. Natl. Acad. Sci. USA 83 (1986) 6622–6626. [DOI] [PMID: 2428037]
3.  Takikawa, O., Yoshida, R., Kido, R. and Hayaishi, O. Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase. J. Biol. Chem. 261 (1986) 3648–3653. [PMID: 2419335]
4.  Hirata, F., Ohnishi, T. and Hayaishi, O. Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex. J. Biol. Chem. 252 (1977) 4637–4642. [PMID: 194886]
5.  Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615–624. [DOI] [PMID: 10719243]
6.  Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525–29531. [DOI] [PMID: 12766158]
7.  Thomas, S.R. and Stocker, R. Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway. Redox Rep. 4 (1999) 199–220. [DOI] [PMID: 10731095]
8.  Sono, M. Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase. Biochemistry 29 (1990) 1451–1460. [PMID: 2334706]
[EC 1.13.11.52 created 2006]
 
 
EC 3.5.1.9     
Accepted name: arylformamidase
Reaction: N-formyl-L-kynurenine + H2O = formate + L-kynurenine
For diagram of tryptophan catabolism, click here
Other name(s): kynurenine formamidase; formylase; formylkynureninase; formylkynurenine formamidase; formamidase I; formamidase II
Systematic name: aryl-formylamine amidohydrolase
Comments: Also acts on other aromatic formylamines.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 156229-75-3
References:
1.  Hayaishi, O. and Stanier, R.Y. The bacterial oxidation of tryptophan. III. Enzymatic activities of cell-free extracts from bacteria employing the aromatic pathway. J. Bacteriol. 62 (1951) 691–709. [PMID: 14907621]
2.  Jakoby, W.B. Kynurenine formamidase from Neurospora. J. Biol. Chem. 207 (1954) 657–663. [PMID: 13163050]
3.  Mehler, A.H. and Knox, W.E. The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine. J. Biol. Chem. 187 (1950) 431–438. [PMID: 14794728]
[EC 3.5.1.9 created 1961]
 
 


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