KMO (gene)

KMO
Identifiers
Aliases	KMO, dJ317G22.1, kynurenine 3-monooxygenase (kynurenine 3-hydroxylase), kynurenine 3-monooxygenase
External IDs	MGI: 2138151 HomoloGene: 2729 GeneCards: KMO
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	241,595,642 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[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 membrane; • extracellular space;
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
	8564
	98256
	ENSG00000117009
	ENSMUSG00000039783
	O15229
	Q91WN4
	NM_003679
	NM_133809
	NP_003670
	NP_598570
	Wikidata
View/Edit Human	View/Edit Mouse

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

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]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000117009 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039783 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: KMO kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)".
↑ 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

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.
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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000117009 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039783 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid9237672-5] 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.

[entrez-6] 1 2 "Entrez Gene: KMO kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)".

[pmid21041030-7] 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

KMO (gene)

References

Further reading