KMO (gene)

Kynurenine 3-monooxygenase is an enzyme that in humans is encoded by the KMO gene.[5][6]

KMO
Identifiers
Aliases	KMO, dJ317G22.1, kynurenine 3-monooxygenase (kynurenine 3-hydroxylase), kynurenine 3-monooxygenase
External IDs	OMIM: 603538 MGI: 2138151 HomoloGene: 2729 GeneCards: KMO
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q43 Start 241,532,134 bp[1] End 241,595,642 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H3 Start 175,620,381 bp[2] End 175,662,116 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • NAD(P)H oxidase activity • monooxygenase activity • oxidoreductase activity • kynurenine 3-monooxygenase activity • flavin adenine dinucleotide binding • FAD binding Cellular component • integral component of membrane • cytosol • membrane • mitochondrial outer membrane • mitochondrion • mitochondrial membranes • extracellular Biological process • pyridine nucleotide biosynthetic process • NAD biosynthetic process • response to salt stress • secondary metabolite biosynthetic process • quinolinate biosynthetic process • tryptophan catabolic process • oxidation-reduction process • response to lipopolysaccharide • cellular response to interleukin-1 • L-kynurenine metabolic process • positive regulation of neuron death • positive regulation of glutamate secretion, neurotransmission • NAD metabolic process • kynurenine metabolic process • 'de novo' NAD biosynthetic process from tryptophan • anthranilate metabolic process • aging • positive regulation of glutamate secretion • kynurenic acid biosynthetic process • cellular response to lipopolysaccharide Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8564	98256
Ensembl	ENSG00000117009	ENSMUSG00000039783
UniProt	O15229	Q91WN4
RefSeq (mRNA)	NM_003679	NM_133809
RefSeq (protein)	NP_003670	NP_598570
Location (UCSC)	Chr 1: 241.53 – 241.6 Mb	Chr 1: 175.62 – 175.66 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Kynurenine 3-monooxygenase (KMO; EC 1.14.13.9) is an NADPH-dependent flavin monooxygenase that catalyzes the hydroxylation of the L-tryptophan metabolite L-kynurenine to form L-3-hydroxykynurenine.[supplied by OMIM][6] This is the first step in the degradation of Kyneurinine to Quinolinic acid. This pathway is involved in the activation of cytokine mediated changes in behavior due to inflammatory stimuli such as infections.[7] The KMO gene is upregulated in the lung parenchyma of smokers. [8]

References

1. GRCh38: Ensembl release 89: ENSG00000117009 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039783 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Alberati-Giani D, Cesura AM, Broger C, Warren WD, Rover S, Malherbe P (Sep 1997). "Cloning and functional expression of human kynurenine 3-monooxygenase". FEBS Lett. 410 (2–3): 407–12. doi:10.1016/S0014-5793(97)00627-3. PMID 9237672. S2CID 26490151.
6. "Entrez Gene: KMO kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)".
7. Dantzer R, O'Connor JC, Lawson MA, Kelley KW (2011), "Inflammation-associated Depression: From Serotonin to Kyneurenine", Psychoneuroendocrinology, 36 (3): 426–36, doi:10.1016/j.psyneuen.2010.09.012, PMC 3053088, PMID 21041030
8. Pintarelli G, Noci S, Maspero D, Pettinicchio A, Dugo M, De Cecco L, Incarbone M, Tosi D, Santambrogio L, Dragani TA, Colombo F (September 2019). "Cigarette smoke alters the transcriptome of non-involved lung tissue in lung adenocarcinoma patients". Scientific Reports. 9 (1): 13039. Bibcode:2019NatSR...913039P. doi:10.1038/s41598-019-49648-2. PMC 6736939. PMID 31506599.

Further reading

• Stone TW, Darlington LG (2002). "Endogenous kynurenines as targets for drug discovery and development". Nature Reviews. Drug Discovery. 1 (8): 609–20. doi:10.1038/nrd870. PMID 12402501. S2CID 19203349.
• Aoyama N, Takahashi N, Saito S, et al. (2006). "Association study between kynurenine 3-monooxygenase gene and schizophrenia in the Japanese population". Genes, Brain and Behavior. 5 (4): 364–8. doi:10.1111/j.1601-183X.2006.00231.x. PMID 16716206.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
• Ligam P, Manuelpillai U, Wallace EM, Walker D (2005). "Localisation of indoleamine 2,3-dioxygenase and kynurenine hydroxylase in the human placenta and decidua: implications for role of the kynurenine pathway in pregnancy". Placenta. 26 (6): 498–504. doi:10.1016/j.placenta.2004.08.009. PMID 15950064.
• 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.
• Halford S, Freedman MS, Bellingham J, et al. (2001). "Characterization of a novel human opsin gene with wide tissue expression and identification of embedded and flanking genes on chromosome 1q43". Genomics. 72 (2): 203–8. doi:10.1006/geno.2001.6469. PMID 11401433.
• Breton J, Avanzi N, Magagnin S, et al. (2000). "Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase". Eur. J. Biochem. 267 (4): 1092–9. doi:10.1046/j.1432-1327.2000.01104.x. PMID 10672018.