Riboflavin kinase catalyzes the phosphorylation of riboflavin to form flavin mononucleotide (FMN), which is an essential step in the biosynthesis of flavin cofactors . These cofactors are vital for various biological processes, including cellular respiration, oxidative stress response, and the metabolism of fats, drugs, and steroids .
The reaction mechanism involves the transfer of a phosphate group from ATP to riboflavin, resulting in the production of FMN and ADP. This reaction is crucial for maintaining the cellular levels of flavin cofactors, which are necessary for the proper functioning of flavoproteins .
Recombinant human riboflavin kinase is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant protein often includes a His-tag to facilitate purification and detection. The purified enzyme is used in various research applications to study its structure, function, and role in different biological processes .
Human riboflavin kinase (HsRFK) is associated with several important physiological and pathological processes. It is involved in protecting cells from oxidative stress and amyloid-β toxicity, which are linked to neurodegenerative diseases such as Alzheimer’s . Additionally, HsRFK expression is related to the progression of certain malignant cancers .
Downregulation of HsRFK can lead to altered expression profiles of clock-controlled metabolic genes and disrupt the protective effects of flavins in stroke treatments . Reduced activity of HsRFK is also associated with protein-energy malnutrition and decreased thyroid hormone levels .
Given its key functions, HsRFK is considered a potential therapeutic target. Understanding the regulation of HsRFK activity and its interaction with other proteins can provide insights into the molecular basis of diseases associated with aberrant HsRFK availability . Furthermore, the differences between human and bacterial RFK enzymes suggest that bacterial RFK could be targeted for developing new antimicrobial agents .