Flavin-dependent dehydrogenase

Flavin-dependent dehydrogenases are a diverse class of oxidoreductase enzymes that utilize flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) as essential cofactors derived from riboflavin (vitamin B2) (UniProt). These enzymes play critical roles in a wide array of metabolic pathways, including the citric acid cycle, fatty acid beta-oxidation, and the metabolism of amino acids and neurotransmitters (PubMed: PMID 29233869). By facilitating the transfer of electrons from a substrate to an electron acceptor, they maintain cellular redox homeostasis and energy production. In clinical medicine, specific members of this family are prominent therapeutic targets; for instance, monoamine oxidases (MAO) are targeted in neuropsychiatric disorders, while lysine-specific demethylase 1 (LSD1) is a focus in oncology for its role in epigenetic regulation (StatPearls: NBK539848). Pharmacological intervention typically involves small-molecule inhibitors that either compete with the substrate or covalently bind to the flavin cofactor, thereby modulating enzymatic activity to treat diseases ranging from Parkinson's disease to various cancers (PubMed: PMID 31536624).

Other names

Flavoprotein dehydrogenaseFAD-dependent dehydrogenaseFMN-dependent dehydrogenaseRiboflavin-dependent oxidoreductase

Inhibition of enzymatic activity through covalent or non-covalent binding to the active site or the flavin cofactor (FAD/FMN), preventing the oxidative deamination or dehydrogenation of substrates (PubMed: PMID 29233869, StatPearls: NBK539848).