FMO2

From Wikipedia, the free encyclopedia

Flavin containing monooxygenase 2 (non-functional)

Identifiers

FMO2; FLJ40826; FMO1B1

External IDs

OMIM: 603955 MGI: 1916776 HomoloGene: 86882

Gene ontology
Molecular Function:	• magnesium ion binding • monooxygenase activity • flavin-containing monooxygenase activity • disulfide oxidoreductase activity • FAD binding • NADP binding
Cellular Component:	• endoplasmic reticulum • microsome • membrane • integral to membrane • intrinsic to endoplasmic reticulum membrane
Biological Process:	• electron transport • oxygen and reactive oxygen species metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001460 (mRNA)
NP_001451 (protein)

NM_018881 (mRNA)
NP_061369 (protein)

Location

Chr 1: 169.42 - 169.45 Mb

Chr 1: 164.71 - 164.74 Mb

Pubmed search

[1]

[2]

Flavin containing monooxygenase 2 (non-functional), also known as FMO2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional).

[edit] Further reading

Hines RN, Cashman JR, Philpot RM, et al. (1994). "The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression.". Toxicol. Appl. Pharmacol. 125 (1): 1–6. doi:10.1006/taap.1994.1042. PMID 8128486.
Dolphin CT, Shephard EA, Povey S, et al. (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. PMID 1417778.
Lomri N, Gu Q, Cashman JR (1992). "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1685–9. PMID 1542660.
Phillips IR, Dolphin CT, Clair P, et al. (1995). "The molecular biology of the flavin-containing monooxygenases of man.". Chem. Biol. Interact. 96 (1): 17–32. PMID 7720101.
Lawton MP, Cashman JR, Cresteil T, et al. (1994). "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.". Arch. Biochem. Biophys. 308 (1): 254–7. PMID 8311461.
McCombie RR, Dolphin CT, Povey S, et al. (1996). "Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q.". Genomics 34 (3): 426–9. 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 Res. 6 (9): 791–806. PMID 8889548.
Dolphin CT, Beckett DJ, Janmohamed A, et al. (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. PMID 9804831.
Whetstine JR, Yueh MF, McCarver DG, et al. (2000). "Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans.". Toxicol. Appl. Pharmacol. 168 (3): 216–24. doi:10.1006/taap.2000.9050. PMID 11042094.
Krueger SK, Martin SR, Yueh MF, et al. (2002). "Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein.". Drug Metab. Dispos. 30 (1): 34–41. PMID 11744609.
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.
Furnes B, Feng J, Sommer SS, Schlenk D (2003). "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans.". Drug Metab. Dispos. 31 (2): 187–93. PMID 12527699.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Krueger SK, Siddens LK, Henderson MC, et al. (2005). "Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics.". Pharmacogenet. Genomics 15 (4): 245–56. PMID 15864117.
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.