Flavin-containing monooxygenase 2 (FMO2)

Flavin-containing monooxygenase 2 (FMO2) is an NADPH-dependent enzyme predominantly responsible for the N-oxidation and S-oxygenation of a broad range of xenobiotics, drugs, and industrial chemicals, especially in pulmonary tissues[4][6]. While FMO2 is catalytically active in most mammals and certain human ethnic groups, the majority of humans (especially Europeans and Asians) possess a non-functional allele resulting in truncated, inactive protein. Functionally, FMO2 protects against cardiac and renal fibrosis by inhibiting TGF-β/SMAD signaling independently of classical oxidoreductase activity and plays a key role in cellular stress responses by acting as an ER chaperone facilitating oxidative protein folding[2][3][5]. Genetic variation in FMO2 impacts drug metabolism and susceptibility to pulmonary toxicity and infection[6]. FMO2’s therapeutic potential is under exploration for preventing or treating cardiac and renal fibrotic remodeling, with possible clinical utility as a biomarker in precision medicine[2][3][5].

Other names

Dimethylaniline monooxygenase [N-oxide-forming] 2FMO 2Dimethylaniline oxidase 2FMO1B1Pulmonary flavin-containing monooxygenase 2Flavin-containing monooxygenase 2 (non-functional)FMOFMO2_HUMANDimethylaniline monooxygenase 2

Catalysis of N-oxidation and S-oxygenation reactions, leading to bioactivation or detoxification of drugs/xenobiotics; Negative regulation of TGF-β/SMAD signaling independently of enzymatic activity; Catalysis of disulfide bond formation, protecting against ER stress–induced apoptosis