FMO4

From Wikipedia, the free encyclopedia

Flavin containing monooxygenase 4

Identifiers

FMO4; FMO2

External IDs

OMIM: 136131 MGI: 2429497 HomoloGene: 68219

Gene ontology
Molecular Function:	• 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 • xenobiotic metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002022 (mRNA)
NP_002013 (protein)

NM_144878 (mRNA)
NP_659127 (protein)

Location

Chr 1: 169.55 - 169.58 Mb

Chr 1: 164.63 - 164.65 Mb

Pubmed search

[1]

[2]

Flavin containing monooxygenase 4, also known as FMO4, is a human gene.^[1]

Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.^[1]

[edit] References

^ ^a ^b Entrez Gene: FMO4 flavin containing monooxygenase 4.

[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.
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.
Itagaki K, Carver GT, Philpot RM (1996). "Expression and characterization of a modified flavin-containing monooxygenase 4 from humans.". J. Biol. Chem. 271 (33): 20102-7. PMID 8702731.
Janmohamed A, Dolphin CT, Phillips IR, Shephard EA (2001). "Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450.". Biochem. Pharmacol. 62 (6): 777-86. PMID 11551524.
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.
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.
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.