Furin convertase enzyme (Furin)

Furin is a calcium-dependent serine protease and a key member of the proprotein convertase family, classified as a subtilisin-like enzyme[1][4][7]. It catalyzes the proteolytic cleavage of a wide range of precursor proteins—such as hormones, growth factors, receptors, and viral glycoproteins—at paired basic amino acid motifs, usually at the Arg-X-Lys/Arg-Arg↓ site[1][4]. The enzyme is synthesized as an inactive zymogen with a prodomain that functions as an intramolecular chaperone and auto-inhibitor, which is cleaved during intracellular trafficking to the trans-Golgi network and endosomal compartments, where it becomes fully active[2][5]. Furin plays a pivotal role in fundamental physiological processes, but its dysregulation is linked to diseases such as cancer, diabetes, cardiovascular disease, and infections, notably facilitating the activation of viral proteins in pathogens like SARS-CoV-2 and HIV[1][3]. Therapeutic targeting of furin is a subject of active research, although the risk of broad physiological disruption is a challenge[1][2][5][7].

Other names

Paired basic amino acid cleaving enzyme (PACE)Proprotein convertase subtilisin/kexin type 3 (PCSK3)

Direct inhibition of proteolytic cleavage activity by binding to the active site or substrate-binding cleft Allosteric inhibition interfering with domain dynamics or substrate access