Rabbit anti-Human FMO5 Polyclonal Antibody

Uniprot Id

P49326

Target Species

Human

Target Name

FMO5

Target Full Name

Flavin-containing monooxygenase 5

Target Function

Acts as Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms (Probable). Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity. Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects.

Target Subcellular Location

Microsome membrane. Endoplasmic reticulum membrane.

Target Protein Families

FMO family

Target Tissue Specificity

Expressed in fetal and adult liver.

Target Synonyms

Dimethylaniline monooxygenase [N oxide forming] 5; Dimethylaniline monooxygenase [N-oxide-forming] 5; Dimethylaniline oxidase 5; FMO 5; FMO5; FMO5_HUMAN; Hepatic flavin containing monooxygenase 5; Hepatic flavin-containing monooxygenase 5

Target Background

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. Alternative splicing results in multiple transcript variants.