KYAT1

Protein-coding gene in the species Homo sapiens
KYAT1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1W7L, 1W7M, 1W7N, 3FVS, 3FVU, 3FVX, 4WLH, 4WLJ, 4WP0

Identifiers
AliasesKYAT1, GTK, KAT1, KATI, CCBL1, kynurenine aminotransferase 1
External IDsOMIM: 600547; MGI: 1917516; HomoloGene: 37872; GeneCards: KYAT1; OMA:KYAT1 - orthologs
EC number4.4.1.13
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[1]
Chromosome 2 (mouse)
Genomic location for KYAT1
Genomic location for KYAT1
Band2|2 BStart30,075,136 bp[1]
End30,095,859 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
    n/a
Top expressed in
  • esophagus

  • right kidney

  • lip

  • left lobe of liver

  • human kidney

  • middle ear

  • Eustachian tube

  • salivary gland

  • seminal vesicula

  • parotid gland
BioGPS
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
  • 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
  • biosynthesis
  • L-kynurenine catabolic process
  • tryptophan catabolic process
  • cellular modified amino acid metabolic process
  • kynurenine metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

883

70266

Ensembl

ENSG00000171097

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/aChr 2: 30.08 – 30.1 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

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.

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. ^ a b c 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. S2CID 83606450.
  5. ^ a b "Entrez Gene: CCBL1 cysteine conjugate-beta lyase; cytoplasmic (glutamine transaminase K, kyneurenine aminotransferase)".

External links

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. S2CID 7643547.
  • 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. doi:10.1042/bst024330s. 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. S2CID 39394531.
  • 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.429..369H. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • 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. S2CID 42325649.
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    1w7l: CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I
  • 1w7m: CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE
    1w7m: CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE
  • 1w7n: CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN PMP FORM
    1w7n: CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN PMP FORM
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