Flavin-dependent oxidoreductase

Flavin-dependent oxidoreductases, or flavoenzymes, are a diverse superfamily of enzymes that utilize flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) as essential redox-active cofactors to catalyze a wide range of biochemical reactions (Massey, 2000, PMID: 11061182). These enzymes are integral to fundamental biological processes, including the citric acid cycle, fatty acid oxidation, and the metabolism of neurotransmitters and xenobiotics (Joosten & van Berkel, 2007, PMID: 17434781). In human health, they play critical roles in maintaining redox homeostasis and regulating gene expression through chromatin-modifying enzymes like Lysine-specific demethylase 1 (LSD1) (UniProt, P61106). Due to their central metabolic and signaling roles, several members are key therapeutic targets; for example, monoamine oxidases (MAO) are targeted in Parkinson's disease and depression, while dihydroorotate dehydrogenase (DHODH) is targeted in autoimmune conditions and cancer (DrugBank, DB01037; DB01097). Pharmacological strategies primarily involve small-molecule inhibitors that either compete with substrates or covalently modify the flavin cofactor to disrupt the catalytic cycle (Pitsikas, 2014, PMID: 24503004).

Other names

FlavoenzymeFlavoproteinFAD-dependent oxidoreductaseFMN-dependent oxidoreductase

Inhibition of enzymatic activity through competitive binding at the substrate site or covalent modification of the flavin cofactor (FAD/FMN).