KYAT1

Kynurenine—oxoglutarate transaminase 1 is an enzyme that in humans is encoded by the CCBL1 gene.[4][5] It is one of the Kynurenine—oxoglutarate transaminases.

KYAT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1W7L, 1W7M, 1W7N, 3FVS, 3FVU, 3FVX, 4WLH, 4WLJ, 4WP0
Identifiers
Aliases	KYAT1, GTK, KAT1, KATI, CCBL1, kynurenine aminotransferase 1
External IDs	OMIM: 600547 MGI: 1917516 HomoloGene: 37872 GeneCards: KYAT1
EC number	4.4.1.13
Gene location (Mouse) Chr. Chromosome 2 (mouse)[1] Band 2|2 B Start 30,185,124 bp[1] End 30,205,847 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • kynurenine-oxoglutarate transaminase activity • protein homodimerization activity • L-glutamine:pyruvate aminotransferase activity • transaminase activity • glutamine-phenylpyruvate transaminase activity • GO:0001948 protein binding • catalytic activity • lyase activity • L-phenylalanine:pyruvate aminotransferase activity • pyridoxal phosphate binding • L-glutamine aminotransferase activity • cysteine-S-conjugate beta-lyase activity Cellular component • nucleoplasm • cytoplasm • cytosol • mitochondrion Biological process • L-phenylalanine catabolic process • cellular amino acid biosynthetic process • biosynthetic process • L-kynurenine catabolic process • tryptophan catabolic process • cellular modified amino acid metabolic process • kynurenine metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	883	70266
Ensembl	n/a	ENSMUSG00000039648
UniProt	Q16773	Q8BTY1
RefSeq (mRNA)	NM_001122671 NM_001122672 NM_001287390 NM_004059	NM_172404 NM_001356474 NM_001356475
RefSeq (protein)	NP_001116143 NP_001116144 NP_001274319 NP_004050 NP_001339917 NP_001339918 NP_001339919 NP_001339920 NP_001339921 NP_001339922 NP_001339923 NP_001339924 NP_001339925 NP_001339926 NP_001339927 NP_001339928	NP_765992 NP_001343403 NP_001343404
Location (UCSC)	n/a	Chr 2: 30.19 – 30.21 Mb
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

This gene encodes a cytosolic enzyme which is responsible for the metabolism of cysteine conjugates of certain halogenated alkenes and alkanes. This metabolism leads to the formation of reactive metabolites which can lead to nephrotoxicity and neurotoxicity.[5]

References

1. GRCm38: Ensembl release 89: ENSMUSG00000039648 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P (Apr 1995). "Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase". FEBS Lett. 360 (3): 277–80. doi:10.1016/0014-5793(95)00123-Q. PMID 7883047.
5. "Entrez Gene: CCBL1 cysteine conjugate-beta lyase; cytoplasmic (glutamine transaminase K, kyneurenine aminotransferase)".

External links

• Human CCBL1 genome location and CCBL1 gene details page in the UCSC Genome Browser.

Further reading

• Cooper AJ (2004). "The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants". Neurochem. Int. 44 (8): 557–77. doi:10.1016/j.neuint.2003.12.002. PMID 15016471.
• Lash LH, Nelson RM, Van Dyke RA, Anders MW (1990). "Purification and characterization of human kidney cytosolic cysteine conjugate beta-lyase activity". Drug Metab. Dispos. 18 (1): 50–4. PMID 2139845.
• Abraham DG, Patel PP, Cooper AJ (1995). "Isolation from rat kidney of a cytosolic high molecular weight cysteine-S-conjugate beta-lyase with activity toward leukotriene E4". J. Biol. Chem. 270 (1): 180–8. doi:10.1074/jbc.270.1.180. PMID 7814371.
• Goldfarb P, Perry S, Harries H, et al. (1996). "Molecular cloning and expression of cDNAs for rat and human kidney cysteine conjugate beta-lyase". Biochem. Soc. Trans. 24 (2): 330S. PMID 8736988.
• Iyer RA, Anders MW (1997). "Cysteine conjugate beta-lyase-dependent biotransformation of the cysteine S-conjugates of the sevoflurane degradation product compound A in human, nonhuman primate, and rat kidney cytosol and mitochondria". Anesthesiology. 85 (6): 1454–61. doi:10.1097/00000542-199612000-00028. PMID 8968194.
• Gilley J, Fried M (1999). "Extensive gene order differences within regions of conserved synteny between the Fugu and human genomes: implications for chromosomal evolution and the cloning of disease genes". Hum. Mol. Genet. 8 (7): 1313–20. doi:10.1093/hmg/8.7.1313. PMID 10369878.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Kapoor R, Lim KS, Cheng A, et al. (2006). "Preliminary evidence for a link between schizophrenia and NMDA-glycine site receptor ligand metabolic enzymes, d-amino acid oxidase (DAAO) and kynurenine aminotransferase-1 (KAT-1)". Brain Res. 1106 (1): 205–10. doi:10.1016/j.brainres.2006.05.082. PMID 16828464.