The Enzyme Database

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EC 1.3.1.18     
Accepted name: kynurenate-7,8-dihydrodiol dehydrogenase
Reaction: 7,8-dihydro-7,8-dihydroxykynurenate + NAD+ = 7,8-dihydroxykynurenate + NADH + H+
Other name(s): 7,8-dihydro-7,8-dihydroxykynurenate dehydrogenase; 7,8-dihydroxykynurenic acid 7,8-diol dehydrogenase
Systematic name: 7,8-dihydro-7,8-dihydroxykynurenate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37255-30-4
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 1.3.1.18 created 1972]
 
 
EC 1.3.99.18     
Accepted name: quinaldate 4-oxidoreductase
Reaction: quinaldate + acceptor + H2O = kynurenate + reduced acceptor
Other name(s): quinaldic acid 4-oxidoreductase
Systematic name: quinoline-2-carboxylate:acceptor 4-oxidoreductase (hydroxylating)
Comments: The enzyme from Pseudomonas sp. AK2 also acts on quinoline-8-carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize nicotinate; quinaldate is a substrate for both of these enzymes. 2,4,6-Trinitrobenzene sulfonate, 1,4-benzoquinone, 1,2-naphthoquinone, nitroblue tetrazolium, thionine and menadione will serve as an electron acceptor for the former enzyme and ferricyanide for the latter; Meldola blue, iodonitrotetrazolium chloride, phenazine methosulfate, 2,6-dichlorophenolindophenol and cytochrome c will act as electron acceptors for both.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 149885-77-8
References:
1.  Sauter, M., Tshisuaka, B., Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases. Biol. Chem. Hoppe Seyler 374 (1993) 1037–1046. [PMID: 8292263]
2.  Fetzner, S. and Lingens, F. Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe-Seyler 374 (1993) 363–376. [PMID: 8357532]
[EC 1.3.99.18 created 1999]
 
 
EC 1.13.1.10      
Transferred entry: Now EC 1.13.11.10, 7,8-dihydroxykynurenate 8,8a-dioxygenase
[EC 1.13.1.10 created 1965, deleted 1972]
 
 
EC 1.13.11.10     
Accepted name: 7,8-dihydroxykynurenate 8,8a-dioxygenase
Reaction: 7,8-dihydroxykynurenate + O2 = 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
Other name(s): 7,8-dihydroxykynurenate oxygenase; 7,8-dihydroxykynurenate 8,8α-dioxygenase; 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing)
Systematic name: 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-58-7
References:
1.  Kuno, S., Tashiro, M., Taniuchi, H., Horibata, K., Hayaishi, O., Seno, S., Tokuyama, T. and Sakan, T. Enzymatic degradation of kynurenic acid. Fed. Proc. 20 (1961) 3.
[EC 1.13.11.10 created 1965 as EC 1.13.1.10, transferred 1972 to EC 1.13.11.10]
 
 
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 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 2.6.1.63     
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, 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]
 
 


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