KMO (gene)

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)
End	241,595,642 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	175,489,682 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; palpebral conjunctiva; ; kidney tubule; ; glomerulus; ; metanephric glomerulus; ; placenta; ; monocyte; ; kidney; ; spleen; ; lymph node;
	Top expressed in
	left lobe of liver; ; kidney; ; proximal tubule; ; spleen; ; blood; ; yolk sac; ; bone marrow; ; Paneth cell; ; subcutaneous adipose tissue; ; thymus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	NAD(P)H oxidase H2O2-forming 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 ; 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 ; ageing ; 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

Last updated January 29, 2023

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] The KMO gene is upregulated in the lung parenchyma of smokers. ^[8]

Related Research Articles

<span class="mw-page-title-main">Kynurenine</span> Chemical compound

l-Kynurenine is a metabolite of the amino acid l-tryptophan used in the production of niacin.

<span class="mw-page-title-main">Aldosterone synthase</span> Protein-coding gene in the species Homo sapiens

Aldosterone synthase, also called steroid 18-hydroxylase, corticosterone 18-monooxygenase or P450C18, is a steroid hydroxylase cytochrome P450 enzyme involved in the biosynthesis of the mineralocorticoid aldosterone and other steroids. The enzyme catalyzes sequential hydroxylations of the steroid angular methyl group at C18 after initial 11β-hydroxylation. It is encoded by the CYP11B2 gene in humans.

Indoleamine-pyrrole 2,3-dioxygenase (IDO or INDO EC 1.13.11.52) is a heme-containing enzyme physiologically expressed in a number of tissues and cells, such as the small intestine, lungs, female genital tract or placenta. In humans is encoded by the IDO1 gene. IDO is involved in tryptophan metabolism. It is one of three enzymes that catalyze the first and rate-limiting step in the kynurenine pathway, the O₂-dependent oxidation of L-tryptophan to N-formylkynurenine, the others being indolamine-2,3-dioxygenase 2 (IDO2) and tryptophan 2,3-dioxygenase (TDO). IDO is an important part of the immune system and plays a part in natural defense against various pathogens. It is produced by the cells in response to inflammation and has an immunosuppressive function because of its ability to limit T-cell function and engage mechanisms of immune tolerance. Emerging evidence suggests that IDO becomes activated during tumor development, helping malignant cells escape eradication by the immune system. Expression of IDO has been described in a number of types of cancer, such as acute myeloid leukemia, ovarian cancer or colorectal cancer. IDO is part of the malignant transformation process and plays a key role in suppressing the anti-tumor immune response in the body, so inhibiting it could increase the effect of chemotherapy as well as other immunotherapeutic protocols.

In enzymology, a kynurenine 3-monooxygenase (EC 1.14.13.9) is an enzyme that catalyzes the chemical reaction

Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene.

Kinesin-like protein KIF2C is a protein that in humans is encoded by the KIF2C gene.

Pleckstrin homology-like domain family A member 2 is a protein that in humans is encoded by the PHLDA2 gene.

Dimethylaniline monooxygenase [N-oxide-forming] 5 is an enzyme that in humans is encoded by the FMO5 gene.

Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.

Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene.

Sodium–hydrogen exchanger 2 is a protein that in humans is encoded by the SLC9A2 gene.

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

Serine/threonine-protein kinase PCTAIRE-3 is an enzyme that in humans is encoded by the PCTK3 gene.

Cytochrome P450 3A43 is a protein that in humans is encoded by the CYP3A43 gene.

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.

Cytochrome P450 2F1 is a protein that in humans is encoded by the CYP2F1 gene.

tRNA isopentenyltransferase, mitochondrial is an enzyme that in humans is encoded by the TRIT1 gene.

Transmembrane protein 222 is a protein that in humans is encoded by the TMEM222 gene. One notable feature of the protein encoded by this gene is the presence of three predicted transmembrane domains. The TMEM222 protein is predicted to most likely localize to the secretory vesicles.

Pappalysin-2 also known as pregnancy-associated plasma protein A2 (PAPP-A2) is a protein that in humans is encoded by the PAPPA2 gene.

CYP8B1 also known as sterol 12-alpha-hydroxylase is a protein which in humans is encoded by the CYP8B1 gene.

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:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
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
↑ 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.

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. Bibcode:2002PNAS...9916899M. 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:". 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.

[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. S2CID 26490151.

[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

[pmid31506599-8] 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.

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KMO (gene)

Related Research Articles

References

Further reading