Kynurenine—oxoglutarate transaminase
| kynurenine-oxoglutarate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.7 | ||||||||
| CAS number | 9030-38-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a kynurenine-oxoglutarate transaminase (EC 2.6.1.7) is an enzyme that catalyzes the chemical reaction
- L-kynurenine + 2-oxoglutarate 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
Thus, the two substrates of this enzyme are L-kynurenine and 2-oxoglutarate, whereas its two products are 4-(2-aminophenyl)-2,4-dioxobutanoate and L-glutamate.
This enzyme belongs to the family of transferases, to be specific, the transaminases, that transfer nitrogenous groups. The systematic name of this enzyme class is L-kynurenine:2-oxoglutarate aminotransferase. Other names in common use include kynurenine transaminase (cyclizing), kynurenine 2-oxoglutarate transaminase, kynurenine aminotransferase, and L-kynurenine aminotransferase. This enzyme participates in tryptophan metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of early 2009, 18 structures have been solved for this class of enzymes, with PDB accession codes 1X0M, 1YIY, 1YIZ, 1W7L, 1W7M, 1W7N, 3E2F, 3E2Y, 3E2Z, 2ZJG, 2YGZ, 2Z61, 2R5C, 2R2N, 2R5E, 3B46, 3DC1, and 2QLN.
References
- BONNER DM, JAKOBY WB (1956). "Kynurenine transaminase from neurospora". J. Biol. Chem. 221 (2): 689–95. PMID 13357462.
- MASON M (1957). "Kynurenine transaminase of rat kidney; a study of coenzyme dissociation". J. Biol. Chem. 227 (1): 61–8. PMID 13449053.
- Rossi F.; Han Q.; Li J.; Li J.; Rizzi M. (2004). "Crystal structure of human kynurenine aminotransferase I". J. Biol. Chem. 279 (48): 50214–20. doi:10.1074/jbc.M409291200. PMID 15364907.
- Chon H.; Matsumura H.; Koga Y.; Takano K.; Kanaya S. (2005). "Crystal structure of a human kynurenine aminotransferase II homologue from Pyrococcus horikoshii OT3 at 2.20 A resolution.". Proteins. 61 (3): 685–8. doi:10.1002/prot.20614. PMID 16138312.
- Han Q.; Gao Y.G.; Robinson H.; Ding H.; Wilson S.; Li J. (2005). "Crystal structures of Aedes aegypti kynurenine aminotransferase.". FEBS J. 272 (9): 2198–206. doi:10.1111/j.1742-4658.2005.04643.x. PMID 15853804.
- Han Q.; Robinson H.; Cai T.; Tagle D.A.; Li J. (2009). "Biochemical and structural properties of mouse KAT III". Mol Cell Biol. 29 (3): 784–93. doi:10.1128/MCB.01272-08. PMC 2630683
. PMID 19029248. - Han Q.; Robinson H.; Li J. (2008). "Crystal structure of human kynurenine aminotransferase II". J. Biol. Chem. 283 (6): 3567–73. doi:10.1074/jbc.M708358200. PMID 18056995.
- Rossi F.; Garavaglia S.; Montalbano V.; Walsh M.A.; Rizzi M. (2008). "Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia.". J. Biol. Chem. 283 (6): 3559–66. doi:10.1074/jbc.M707925200. PMID 18056996.
- Han Q.; Cai T.; Tagle D.A.; Robinson H.; Li J. (2008). "Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II.". Biosci Rep. 28 (4): 205–15. doi:10.1042/BSR20080085. PMC 2559858. PMID 18620547.
- Han Q.; Gao Y.G.; Robinson H.; Li J. (2008). "Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.". Biochemistry. 47 (6): 1622–30. doi:10.1021/bi701800j. PMC 2858008. PMID 18186649.
- Wogulis M.; Chew E.R.; Donohoue P.D.; Wilson D.K. (2008). "Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence.". Biochemistry. 47 (6): 1608–21. doi:10.1021/bi701172v. PMID 18205391.