Flavin Mononucleotide-Dependent Enzyme

Flavin mononucleotide-dependent enzymes are a class of oxidoreductases that utilize flavin mononucleotide (FMN) as a prosthetic group or cofactor to catalyze redox reactions. FMN, also known as riboflavin-5′-phosphate, is derived from riboflavin (vitamin B2). These enzymes play essential roles in cellular metabolism and are involved in various physiological processes. FMN acts as an electron carrier, cycling between oxidized (FMN), semiquinone (FMNH•), and reduced (FMNH₂) states during catalysis. They can participate in both one-electron and two-electron transfer reactions. Examples include NADH dehydrogenase and lactate oxidase. They are crucial for energy production, fatty acid oxidation, amino acid metabolism, and cellular defense against oxidative stress. Deficiency or dysfunction can lead to metabolic disorders, and differences in biosynthetic pathways in pathogens present opportunities for drug targeting.

Inhibition of enzymatic activity