FMO2

FMO2
Identifiers
Aliases	FMO2, FMO1B1, flavin containing monooxygenase 2, flavin containing dimethylaniline monoxygenase 2
External IDs	OMIM: 603955; MGI: 1916776; HomoloGene: 86882; GeneCards: FMO2; OMA:FMO2 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	171,212,686 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	162,726,295 bp
RNA expression pattern
	Top expressed in
	pericardium; ; right lung; ; lower lobe of lung; ; Descending thoracic aorta; ; lactiferous duct; ; ascending aorta; ; vena cava; ; upper lobe of lung; ; upper lobe of left lung; ; abdominal fat;
	Top expressed in
	lumbar spinal ganglion; ; ascending aorta; ; right lung; ; left lung lobe; ; aortic valve; ; right lung lobe; ; pericardium; ; esophagus; ; right kidney; ; human kidney;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; N,N-dimethylaniline monooxygenase activity; NADP binding; flavin adenine dinucleotide binding; monooxygenase activity;
Cellular component	organelle membrane; endoplasmic reticulum membrane; membrane; endoplasmic reticulum; intracellular membrane-bounded organelle;
Biological process	xenobiotic metabolic process; toxin metabolic process; NADPH oxidation; NADP metabolic process; oxygen metabolic process; organic acid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	2327
	55990
	ENSG00000094963
	ENSMUSG00000040170
	Q99518
	Q8K2I3
	NM_001301347; NM_001460; NM_001365900
	NM_018881; NM_001360913; NM_001360914
	NP_001288276; NP_001451; NP_001352829
	NP_061369; NP_001347842; NP_001347843
	Wikidata
View/Edit Human	View/Edit Mouse

Flavin-containing monooxygenase 2 (FMO2), also known as dimethylaniline monooxygenase [N-oxide-forming] 2, is a mammalian enzyme that in humans is encoded by the FMO2 gene.⁵⁶⁷ The gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.⁷

FMO2 is a member of the family of flavin-containing monooxygenases, NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. It catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate.⁷

In humans, FMO2 is expressed in lung tissue.⁸ The most common isoform, FMO2*2A, contains a premature stop codon, leading to a truncated protein with no catalytic activity that is probably rapidly degraded.⁷ The other isoform, FMO2*1, present in sub-Saharan Africans (up to 50%), African-Americans (26%) and Hispanics (2–7%), is functional.⁸⁹ Its substrates include thioether-containing pesticides, the anti-tuberculosis drug ethionamide, as well as α-naphthylthiourea and other thioureas.⁹

References

GRCh38: Ensembl release 89: ENSG00000094963 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000040170 – 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.
Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (Nov 1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". The Biochemical Journal. 287. ( Pt 1) (Pt 1): 261–267. doi:10.1042/bj2870261. PMC 1133153. PMID 1417778.
Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, et al. (Dec 1998). "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein". The Journal of Biological Chemistry. 273 (46): 30599–30607. doi:10.1074/jbc.273.46.30599. PMID 9804831.
"Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)".
Online Mendelian Inheritance in Man (OMIM): 603955
Veeramah KR, Thomas MG, Weale ME, Zeitlyn D, Tarekegn A, Bekele E, et al. (October 2008). "The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa". Pharmacogenetics and Genomics. 18 (10): 877–886. doi:10.1097/fpc.0b013e3283097311. PMC 2666332. PMID 18794725.

Further reading

Hines RN, Cashman JR, Philpot RM, Williams DE, Ziegler DM (March 1994). "The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression". Toxicology and Applied Pharmacology. 125 (1): 1–6. doi:10.1006/taap.1994.1042. PMID 8128486.
Lomri N, Gu Q, Cashman JR (1992). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver". Proceedings of the National Academy of Sciences of the United States of America. 89 (5): 1685–1689. Bibcode:1992PNAS...89.1685L. doi:10.1073/pnas.89.5.1685. PMC 48517. PMID 1542660.
Phillips IR, Dolphin CT, Clair P, Hadley MR, Hutt AJ, McCombie RR, et al. (April 1995). "The molecular biology of the flavin-containing monooxygenases of man". Chemico-Biological Interactions. 96 (1): 17–32. Bibcode:1995CBI....96...17P. doi:10.1016/0009-2797(94)03580-2. PMID 7720101.
Lawton MP, Cashman JR, Cresteil T, Dolphin CT, Elfarra AA, Hines RN, et al. (January 1994). "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities". Archives of Biochemistry and Biophysics. 308 (1): 254–257. doi:10.1006/abbi.1994.1035. PMID 8311461.
McCombie RR, Dolphin CT, Povey S, Phillips IR, Shephard EA (June 1996). "Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q". Genomics. 34 (3): 426–429. doi:10.1006/geno.1996.0308. PMID 8786146.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Whetstine JR, Yueh MF, McCarver DG, Williams DE, Park CS, Kang JH, et al. (November 2000). "Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans". Toxicology and Applied Pharmacology. 168 (3): 216–224. doi:10.1006/taap.2000.9050. PMID 11042094.
Krueger SK, Martin SR, Yueh MF, Pereira CB, Williams DE (January 2002). "Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein". Drug Metabolism and Disposition. 30 (1): 34–41. doi:10.1124/dmd.30.1.34. PMID 11744609. S2CID 9151632.
Furnes B, Feng J, Sommer SS, Schlenk D (2003). "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans". Drug Metabolism and Disposition. 31 (2): 187–193. doi:10.1124/dmd.31.2.187. PMID 12527699. S2CID 6619389.
Krueger SK, Siddens LK, Henderson MC, Andreasen EA, Tanguay RL, Pereira CB, et al. (April 2005). "Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics". Pharmacogenetics and Genomics. 15 (4): 245–256. doi:10.1097/01213011-200504000-00008. PMC 1351039. PMID 15864117.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000094963 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040170 – 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.

[pmid1417778-5] Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (Nov 1992). "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family". The Biochemical Journal. 287. ( Pt 1) (Pt 1): 261–267. doi:10.1042/bj2870261. PMC 1133153. PMID 1417778.

[pmid9804831-6] Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, et al. (Dec 1998). "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein". The Journal of Biological Chemistry. 273 (46): 30599–30607. doi:10.1074/jbc.273.46.30599. PMID 9804831.

[entrez-7] "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)".

[OMIM-8] Online Mendelian Inheritance in Man (OMIM): 603955

[Veeramah2008-9] Veeramah KR, Thomas MG, Weale ME, Zeitlyn D, Tarekegn A, Bekele E, et al. (October 2008). "The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa". Pharmacogenetics and Genomics. 18 (10): 877–886. doi:10.1097/fpc.0b013e3283097311. PMC 2666332. PMID 18794725.

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