Riboflavin kinase (RFK)

Riboflavin kinase (RFK) is an essential enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN), which is a precursor for flavin adenine dinucleotide (FAD), both of which are fundamental cofactors in cellular redox biology and metabolism[1][2][5]. Human RFK shows a unique beta-barrel fold and active site arrangement optimized for binding ATP and riboflavin, enabling efficient phosphoryl transfer[1]. As the rate-limiting enzyme in the synthesis of FAD, RFK is crucial in numerous metabolic and oxidative stress pathways. It also plays a role in tumor necrosis factor (TNF)-induced ROS production via NADPH oxidase activation, and thus is implicated in the regulation of oxidative stress and the potential development of related disorders. Given its central role in flavin metabolism and cellular redox homeostasis, RFK is a prospective therapeutic target for conditions involving aberrant oxidative or metabolic processes[3][5].

Other names

ATP:riboflavin 5'-phosphotransferaseFlavokinaseRFK

Enzyme inhibition (targeting RFK would block riboflavin conversion to FMN/FAD leading to altered flavoprotein-dependent metabolic pathways)[3]