FMO1
FMO1 (flavin-containing monooxygenase 1) is a broad-spectrum, NADPH-dependent flavoenzyme of the endoplasmic reticulum membrane. It oxygenates a wide variety of nitrogen- and sulfur-containing compounds, including xenobiotics, and is a member of the FMO family. Browse Assay Genie's current range of FMO1 research reagents below, or read on for the biology behind the target.
FMO1 is a broad-spectrum monooxygenase that catalyses the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds, including xenobiotics. Like other flavin-containing monooxygenases, it is an NADPH-dependent flavoenzyme that oxidises soft nucleophilic heteroatom centres in drugs, pesticides and other foreign compounds. It catalyses the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation and in a variety of cytoprotective and developmental processes.
In vitro, FMO1 catalyses the N-oxygenation of trimethylamine (TMA) to trimethylamine N-oxide (TMAO), and could therefore contribute to detoxification of TMA. TMA is generated by gut microbiota from dietary precursors such as choline, choline-containing compounds, betaine or L-carnitine. The protein is located in the endoplasmic reticulum membrane. Two EC numbers are assigned to it, reflecting these activities.
The human FMO1 gene belongs to the FMO family and sits in a cluster with related genes in the 1q23-q25 region. According to the NCBI Gene summary, FMO1 is the form found in foetal liver, FMO2 is found in adult liver, and FMO3 is the third member of the cluster. An inherited FMO3 polymorphism reduces TMA N-oxidation capacity in a small subpopulation and causes the fish odour syndrome trimethylaminuria. Several transcript variants encoding different isoforms have been reported for this gene. The previous HGNC name was flavin containing monooxygenase 1, and mouse and rat each carry an Fmo1 ortholog.
FMO1 oxidises soft nucleophilic heteroatom centres in drugs, pesticides and other xenobiotics, making it relevant to studies of foreign-compound handling.
In vitro, FMO1 converts trimethylamine to TMAO, linking it to detoxification of a compound derived from gut microbiota and dietary precursors.
FMO1 catalyses S-oxygenation of hypotaurine to taurine, an osmolyte involved in cell volume regulation and cytoprotective and developmental processes.
FMO1 is the form found in foetal liver, in contrast to FMO2 in adult liver, which makes it useful for comparing FMO family expression.
FMO1 is a broad-spectrum monooxygenase that oxygenates nitrogen- and sulfur-containing compounds, including xenobiotics. It converts hypotaurine to taurine and, in vitro, trimethylamine to trimethylamine N-oxide. Like other FMOs, it is an NADPH-dependent flavoenzyme acting on soft nucleophilic heteroatom centres.
FMO1, FMO2 and FMO3 are encoded by genes clustered in the 1q23-q25 region. FMO1 is found in foetal liver and FMO2 in adult liver. An inherited FMO3 polymorphism is linked to trimethylaminuria, a fish odour syndrome.
Yes, mouse and rat each have an Fmo1 ortholog. Several transcript variants encoding different isoforms have been found for the human gene. Check the datasheet of any product for its validated reactivity.
Other flavin-containing monooxygenase family members and similarly named targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q01740; product specifications from Assay Genie datasheets.