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 1.13.11.42      
Deleted entry:  indoleamine-pyrrole 2,3-dioxygenase. The enzyme was identical to EC 1.13.11.11, tryptophan 2,3-dioxygenase
[EC 1.13.11.42 created 1992, deleted 2006]
 
 
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 1.14.1.2      
Transferred entry: now EC 1.14.13.9, kynurenine 3-monooxygenase
[EC 1.14.1.2 created 1965, deleted 1972]
 
 
EC 1.14.1.4      
Transferred entry: now EC 1.14.99.2, kynurenine 7,8-hydroxylase
[EC 1.14.1.4 created 1965, deleted 1972]
 
 
EC 1.14.13.9     
Accepted name: kynurenine 3-monooxygenase
Reaction: L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O
For diagram of tryptophan catabolism, click here
Other name(s): kynurenine 3-hydroxylase; kynurenine hydroxylase; L-kynurenine-3-hydroxylase
Systematic name: L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-61-2
References:
1.  de Castro, F.T., Price, J.M. and Brown, R.R. Reduced triphosphopyridinenucleotide requirement for the enzymatic formation of 3-hydroxykynurenine from L-kynurenine. J. Am. Chem. Soc. 78 (1956) 2904–2905.
2.  Okamoto, H. and Hayaishi, O. Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria. Biochem. Biophys. Res. Commun. 29 (1967) 394–399. [DOI] [PMID: 6076241]
3.  Saito, Y., Hayaishi, O. and Rothberg, S. Studies on oxygenases: enzymatic formation of 3-hydroxy-L-kynurenine from L-kynurenine. J. Biol. Chem. 229 (1957) 921–934. [PMID: 13502353]
[EC 1.14.13.9 created 1961 as EC 1.99.1.5, transferred 1965 to EC 1.14.1.2, transferred 1972 to EC 1.14.13.9]
 
 
EC 1.14.99.2     
Accepted name: kynurenine 7,8-hydroxylase
Reaction: kynurenate + reduced acceptor + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + acceptor
Other name(s): kynurenic acid hydroxylase; kynurenic hydroxylase; kynurenate 7,8-hydroxylase
Systematic name: kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-63-4
References:
1.  Taniuchi, H. and Hayaishi, O. Studies on the metabolism of kynurenic acid. III. Enzymatic formation of 7,8-dihydroxykynurenic acid from kynurenic acid. J. Biol. Chem. 238 (1963) 283–293. [PMID: 13984873]
[EC 1.14.99.2 created 1965 as EC 1.14.1.4, transferred 1972 to EC 1.14.99.2]
 
 
EC 1.99.1.5      
Transferred entry: Now EC 1.14.13.9, kynurenine 3-monooxygenase
[EC 1.99.1.5 created 1961, deleted 1965]
 
 
EC 2.6.1.7     
Accepted name: kynurenine—oxoglutarate transaminase
Reaction: L-kynurenine + 2-oxoglutarate = kynurenate + L-glutamate + H2O (overall reaction)
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
(1b) 4-(2-aminophenyl)-2,4-dioxobutanoate = kynurenate + H2O (spontaneous)
For diagram of EC 2.6.1, click here and for diagram of tryptophan catabolism, click here
Glossary: kynurenine = 2-amino-4-(2-aminophenyl)-4-oxobutanoic acid = 3-anthraniloylalanine
kynurenate = 4-hydroxyquinoline-2-carboxylate
Other name(s): kynurenine transaminase (cyclizing); kynurenine 2-oxoglutarate transaminase; kynurenine aminotransferase; L-kynurenine aminotransferase
Systematic name: L-kynurenine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 3-hydroxykynurenine. The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-38-0
References:
1.  Jakoby, W.B. and Bonner, D.M. Kynurenine transaminase from Neurospora. J. Biol. Chem. 221 (1956) 689–695. [PMID: 13357462]
2.  Mason, M. Kynurenine transaminase of rat kidney: a study of coenzyme dissociation. J. Biol. Chem. 227 (1957) 61–68. [PMID: 13449053]
3.  Noguchi, T., Minatogawa, Y., Okuno, E., Nakatani, M. and Morimoto, M. Purification and characterization of kynurenine—2-oxoglutarate aminotransferase from the liver, brain and small intestine of rats. Biochem. J. 151 (1975) 399–406. [DOI] [PMID: 1218085]
4.  Han, Q., Cai, T., Tagle, D.A., Robinson, H. and Li, J. Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep 28 (2008) 205–215. [DOI] [PMID: 18620547]
5.  Han, Q., Robinson, H., Cai, T., Tagle, D.A. and Li, J. Biochemical and structural properties of mouse kynurenine aminotransferase III. Mol. Cell Biol. 29 (2009) 784–793. [DOI] [PMID: 19029248]
[EC 2.6.1.7 created 1961, modified 1983]
 
 
EC 2.6.1.60     
Accepted name: aromatic-amino-acid—glyoxylate transaminase
Reaction: an aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine
Systematic name: aromatic-amino-acid:glyoxylate aminotransferase
Comments: Phenylalanine, kynurenine, tyrosine and histidine can act as amino donors; glyoxylate, pyruvate and hydroxypyruvate can act as amino acceptors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67185-76-6
References:
1.  Harada, I., Noguchi, T. and Kido, R. Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver. Hoppe-Seylers Z. Physiol. Chem. 359 (1978) 481–488. [DOI] [PMID: 25837]
[EC 2.6.1.60 created 1978]
 
 
EC 2.6.1.63     
Accepted name: kynurenine—glyoxylate transaminase
Reaction: (1) L-kynurenine + glyoxylate = kynurenate + glycine + H2O (overall reaction)
(1a) L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
(1b) 4-(2-aminophenyl)-2,4-dioxobutanoate = kynurenate + H2O (spontaneous)
(2) 3-hydroxy-L-kynurenine + glyoxylate = xanthurenate + glycine + H2O (overall reaction)
(2a) 3-hydroxy-L-kynurenine + glyoxylate = 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate + glycine
(2b) 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate = xanthurenate + H2O (spontaneous)
For diagram of EC 2.6.1, click here
Other name(s): kynurenine-glyoxylate aminotransferase
Systematic name: L-kynurenine:glyoxylate aminotransferase (cyclizing)
Comments: This enzyme, characterized from animals, belongs to a family of aminotransferases some members of which can use other amino acceptors (cf. EC 2.6.1.7, kynurenine—oxoglutarate transaminase). The products, 4-(2-aminophenyl)-2,4-dioxobutanoate and 4-(2-amino-3-hydroxyphenyl)-2,4-dioxobutanoate, are converted to kynurenate and xanthurenate, respectively, by spontaneous reactions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74506-33-5
References:
1.  Harada, I., Noguchi, T. and Kido, R. Purification and characterization of aromatic-amino-acid-glyoxylate aminotransferase from monkey and rat liver. Hoppe-Seylers Z. Physiol. Chem. 359 (1978) 481–488. [DOI] [PMID: 25837]
2.  Harada, I. [Glucagen inducible kynurenine aminotransferase.] Wakayama Igaku 31 (1980) 61–68. (in Japanese)
3.  Han, Q., Fang, J. and Li, J. 3-Hydroxykynurenine transaminase identity with alanine glyoxylate transaminase. A probable detoxification protein in Aedes aegypti. J. Biol. Chem. 277 (2002) 15781–15787. [DOI] [PMID: 11880382]
4.  Rossi, F., Lombardo, F., Paglino, A., Cassani, C., Miglio, G., Arca, B. and Rizzi, M. Identification and biochemical characterization of the Anopheles gambiae 3-hydroxykynurenine transaminase. FEBS J. 272 (2005) 5653–5662. [DOI] [PMID: 16262702]
[EC 2.6.1.63 created 1983]
 
 
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, PDB, 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]
 
 
EC 3.7.1.3     
Accepted name: kynureninase
Reaction: L-kynurenine + H2O = anthranilate + L-alanine
For diagram of tryptophan catabolism, click here
Systematic name: L-kynurenine hydrolase
Comments: A pyridoxal-phosphate protein. Also acts on 3′-hydroxy-L-kynurenine and some other (3-arylcarbonyl)-alanines.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-78-6
References:
1.  Jakoby, W.B. and Bonner, D.M. Kynureninase from Neurospora: purification and properties. J. Biol. Chem. 205 (1953) 699–707. [PMID: 13129248]
2.  Jakoby, W.B. and Bonner, D.M. Kynureninase from Neurospora: interactions of enzyme with substrates, coenzyme and amines. J. Biol. Chem. 205 (1953) 709–715. [PMID: 13129249]
3.  Knox, W.E. The relation of liver kynureninase to tryptophan metabolism in pyridoxine deficiency. Biochem. J. 53 (1953) 379–385. [PMID: 13032082]
4.  Wiss, O. and Weber, F. Die Reindarstellung der Kynureninase. Hoppe-Seyler's Z. Physiol. Chem. 304 (1956) 232–240.
[EC 3.7.1.3 created 1965]
 
 


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