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{{Infobox_gene}}
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'''Dimethylaniline monooxygenase [N-oxide-forming] 2''' is an [[enzyme]] that in humans is encoded by the ''FMO2'' [[gene]].<ref name="pmid1417778">{{cite journal |vauthors=Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR | title = Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family | series = 287 | journal = Biochem J | volume = ( Pt 1) | issue =  | pages = 261–7 |date=Nov 1992 | pmid = 1417778 | pmc = 1133153 | doi = }}</ref><ref name="pmid9804831">{{cite journal |vauthors=Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR | title = The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein | journal = J Biol Chem | volume = 273 | issue = 46 | pages = 30599–607 |date=Dec 1998 | pmid = 9804831 | pmc =  | doi =10.1074/jbc.273.46.30599 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2327| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Flavin containing monooxygenase 2 (non-functional)
| HGNCid = 3770
| Symbol = FMO2
| AltSymbols =; FLJ40826; FMO1B1
| OMIM = 603955
| ECnumber =
  | Homologene = 86882
| MGIid = 1916776
| GeneAtlas_image1 = PBB_GE_FMO2_211726_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004499 |text = flavin-containing monooxygenase activity}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0031227 |text = intrinsic to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006800 |text = oxygen and reactive oxygen species metabolic process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2327
    | Hs_Ensembl = ENSG00000094963
    | Hs_RefseqProtein = NP_001451
    | Hs_RefseqmRNA = NM_001460
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 169420971
    | Hs_GenLoc_end = 169448171
    | Hs_Uniprot = Q99518
    | Mm_EntrezGene = 55990
    | Mm_Ensembl = ENSMUSG00000040170
    | Mm_RefseqmRNA = NM_018881
    | Mm_RefseqProtein = NP_061369
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 164711722
    | Mm_GenLoc_end = 164735387
    | Mm_Uniprot = Q8K2I3
  }}
}}
'''Flavin containing monooxygenase 2 (non-functional)''', also known as '''FMO2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2327| accessdate = }}</ref>


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{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.<ref name="entrez">{{cite web | title = Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2327| accessdate = }}</ref>
| summary_text = The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Hines RN, Cashman JR, Philpot RM, ''et al.'' |title=The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression. |journal=Toxicol. Appl. Pharmacol. |volume=125 |issue= 1 |pages= 1-6 |year= 1994 |pmid= 8128486 |doi= 10.1006/taap.1994.1042 }}
*{{cite journal  |vauthors=Hines RN, Cashman JR, Philpot RM |title=The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression. |journal=Toxicol. Appl. Pharmacol. |volume=125 |issue= 1 |pages= 1–6 |year= 1994 |pmid= 8128486 |doi= 10.1006/taap.1994.1042 |display-authors=etal}}
*{{cite journal  | author=Dolphin CT, Shephard EA, Povey S, ''et al.'' |title=Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family. |journal=Biochem. J. |volume=287 ( Pt 1) |issue=  |pages= 261-7 |year= 1992 |pmid= 1417778 |doi=  }}
*{{cite journal  |vauthors=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1685–9 |year= 1992 |pmid= 1542660 |doi=10.1073/pnas.89.5.1685  | pmc=48517 }}
*{{cite journal  | author=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1685-9 |year= 1992 |pmid= 1542660 |doi=  }}
*{{cite journal  |vauthors=Phillips IR, Dolphin CT, Clair P |title=The molecular biology of the flavin-containing monooxygenases of man. |journal=Chem. Biol. Interact. |volume=96 |issue= 1 |pages= 17–32 |year= 1995 |pmid= 7720101 |doi=10.1016/0009-2797(94)03580-2 |display-authors=etal}}
*{{cite journal  | author=Phillips IR, Dolphin CT, Clair P, ''et al.'' |title=The molecular biology of the flavin-containing monooxygenases of man. |journal=Chem. Biol. Interact. |volume=96 |issue= 1 |pages= 17-32 |year= 1995 |pmid= 7720101 |doi=  }}
*{{cite journal  |vauthors=Lawton MP, Cashman JR, Cresteil T |title=A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities. |journal=Arch. Biochem. Biophys. |volume=308 |issue= 1 |pages= 254–7 |year= 1994 |pmid= 8311461 |doi=10.1006/abbi.1994.1035 |display-authors=etal}}
*{{cite journal  | author=Lawton MP, Cashman JR, Cresteil T, ''et al.'' |title=A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities. |journal=Arch. Biochem. Biophys. |volume=308 |issue= 1 |pages= 254-7 |year= 1994 |pmid= 8311461 |doi=  }}
*{{cite journal  |vauthors=McCombie RR, Dolphin CT, Povey S |title=Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q. |journal=Genomics |volume=34 |issue= 3 |pages= 426–9 |year= 1996 |pmid= 8786146 |doi= 10.1006/geno.1996.0308 |display-authors=etal}}
*{{cite journal  | author=McCombie RR, Dolphin CT, Povey S, ''et al.'' |title=Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q. |journal=Genomics |volume=34 |issue= 3 |pages= 426-9 |year= 1996 |pmid= 8786146 |doi= 10.1006/geno.1996.0308 }}
*{{cite journal  |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal  |vauthors=Whetstine JR, Yueh MF, McCarver DG |title=Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans. |journal=Toxicol. Appl. Pharmacol. |volume=168 |issue= 3 |pages= 216–24 |year= 2000 |pmid= 11042094 |doi= 10.1006/taap.2000.9050 |display-authors=etal}}
*{{cite journal  | author=Dolphin CT, Beckett DJ, Janmohamed A, ''et al.'' |title=The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30599-607 |year= 1998 |pmid= 9804831 |doi= }}
*{{cite journal  |vauthors=Krueger SK, Martin SR, Yueh MF |title=Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein. |journal=Drug Metab. Dispos. |volume=30 |issue= 1 |pages= 34–41 |year= 2002 |pmid= 11744609 |doi=10.1124/dmd.30.1.34 |display-authors=etal}}
*{{cite journal  | author=Whetstine JR, Yueh MF, McCarver DG, ''et al.'' |title=Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans. |journal=Toxicol. Appl. Pharmacol. |volume=168 |issue= 3 |pages= 216-24 |year= 2000 |pmid= 11042094 |doi= 10.1006/taap.2000.9050 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Krueger SK, Martin SR, Yueh MF, ''et al.'' |title=Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein. |journal=Drug Metab. Dispos. |volume=30 |issue= 1 |pages= 34-41 |year= 2002 |pmid= 11744609 |doi=  }}
*{{cite journal  |vauthors=Furnes B, Feng J, Sommer SS, Schlenk D |title=Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. |journal=Drug Metab. Dispos. |volume=31 |issue= 2 |pages= 187–93 |year= 2003 |pmid= 12527699 |doi=10.1124/dmd.31.2.187 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Furnes B, Feng J, Sommer SS, Schlenk D |title=Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. |journal=Drug Metab. Dispos. |volume=31 |issue= 2 |pages= 187-93 |year= 2003 |pmid= 12527699 |doi=  }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Krueger SK, Siddens LK, Henderson MC |title=Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics. |journal=Pharmacogenet. Genomics |volume=15 |issue= 4 |pages= 245–56 |year= 2005 |pmid= 15864117 |doi=10.1097/01213011-200504000-00008  | pmc=1351039 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |display-authors=etal}}
*{{cite journal  | author=Krueger SK, Siddens LK, Henderson MC, ''et al.'' |title=Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics. |journal=Pharmacogenet. Genomics |volume=15 |issue= 4 |pages= 245-56 |year= 2005 |pmid= 15864117 |doi=  }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
}}
{{refend}}
{{refend}}


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{{Dioxygenases}}
 
 
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Latest revision as of 04:52, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Wikidata
View/Edit Human

Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene.[1][2][3]

The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein encoded by this gene represents the truncated form and apparently has no catalytic activity. A functional allele found in African Americans has been reported, but no sequence evidence has been deposited to support the finding. This gene is found in a cluster with the FMO1, FMO3, and FMO4 genes on chromosome 1.[3]

References

  1. ↑ 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". Biochem J. 287. ( Pt 1): 261–7. PMC 1133153. PMID 1417778.
  2. ↑ Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR (Dec 1998). "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein". J Biol Chem. 273 (46): 30599–607. doi:10.1074/jbc.273.46.30599. PMID 9804831.
  3. ↑ 3.0 3.1 "Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)".

Further reading



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