Nitrilase family member 2 (NIT2)

Nitrilase family member 2 (NIT2) is a mammalian enzyme and member of the nitrilase superfamily, a group of thiol enzymes that catalyze hydrolysis of C-N bonds. NIT2, also known as nitrilase-2 or omega-amidase, is involved in cellular metabolism of asparagine, glutamine, and oxaloacetate and is found in the cytosol and centrosome[5]. Structurally, NIT2 has a four-layered α/β/β/α fold typical of nitrilase enzymes and features a catalytic triad consisting of glutamate, lysine, and cysteine residues[1][3]. Although the physiological substrates and specific inhibitors of NIT2 are not well defined, some studies suggest distinct biological functions, including a role in cell growth regulation and possible tumor suppression[1]. NIT2 is considered an enzyme target, with roles in intermediary metabolism and the innate immune system. Currently, there are no established drugs or biomarkers directly associated with NIT2, and detailed clinical or safety data are lacking.

Other names

Nit2omega-amidasenitrilase-2

Enzymatic hydrolysis of carbon-nitrogen bonds (omega-amidase activity)