Cytochrome b5 reductase 2 (CYB5R2)

Cytochrome b5 reductase 2 (CYB5R2) is a member of the flavoprotein pyridine nucleotide cytochrome reductase family of enzymes, functioning as an oxidoreductase that uses NADH to catalyze the reduction of cytochrome b5 and other substrates[3][6]. While most intensively studied for its roles in lipid metabolism—including fatty acid desaturation, elongation, and cholesterol biosynthesis—CYB5R2 is also implicated in redox regulation and is predicted to be expressed mainly in tissues such as testis and tibial nerve[3][5]. Like other family members, CYB5R2 possesses both FAD and NADH-binding domains, enabling electron transfer critical for various metabolic pathways. Compared to the paralog CYB5R3, much less is known about the precise physiological and pathological roles of CYB5R2; disease associations are emerging but not yet definitive[3][4][5]. No approved drugs are currently known to target CYB5R2 specifically, and it is primarily considered a potential rather than an established therapeutic target.

Other names

NADH-cytochrome b5 reductase 2b5R.2B5R.2cytochrome b5 reductase b5R.2CYB5R2

Electron transfer from NADH to cytochrome b5, which thereafter participates in various metabolic and biosynthetic reactions[1][6][7]