KMO (gene)

From Wikipedia, the free encyclopedia

Kynurenine 3-monooxygenase (kynurenine 3-hydroxylase)

Identifiers

KMO; dJ317G22.1

External IDs

OMIM: 603538 MGI: 2138151 HomoloGene: 2729

Gene ontology
Molecular Function:	• monooxygenase activity • kynurenine 3-monooxygenase activity • electron carrier activity
Cellular Component:	• mitochondrion • mitochondrial inner membrane • membrane • integral to membrane
Biological Process:	• electron transport • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003679 (mRNA)
NP_003670 (protein)

NM_133809 (mRNA)
NP_598570 (protein)

Location

Chr 1: 239.76 - 239.83 Mb

Chr 1: 177.46 - 177.5 Mb

Pubmed search

[1]

[2]

Kynurenine 3-monooxygenase (kynurenine 3-hydroxylase), also known as KMO, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: KMO kynurenine 3-monooxygenase (kynurenine 3-hydroxylase).

[edit] Further reading

Stone TW, Darlington LG (2002). "Endogenous kynurenines as targets for drug discovery and development.". Nature reviews. Drug discovery 1 (8): 609-20. 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 Behav. 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.
Aoyama N, Takahashi N, Saito S, et al.. "Association study between kynurenine 3-monooxygenase gene and schizophrenia in the Japanese population.". Genes Brain Behav.. doi:10.1111/j.1601-183X.2006.00231.x. PMID 16643513.
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. 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. PMID 10672018.
Alberati-Giani D, Cesura AM, Broger C, et al. (1997). "Cloning and functional expression of human kynurenine 3-monooxygenase.". FEBS Lett. 410 (2-3): 407-12. PMID 9237672.