Carnosine dipeptidase 1 (CNDP1)

Carnosine dipeptidase 1 (CNDP1), commonly referred to as human serum carnosinase or CN1, is a secreted homodimeric dipeptidase belonging to the M20 metallopeptidase family. It catalyzes the hydrolysis of histidine-containing dipeptides, most notably carnosine, a molecule with antioxidant, anti-inflammatory, and anti–advanced glycation end-product (AGE) functions. CNDP1 is predominantly expressed in the brain and serum, and its genetic polymorphisms can affect enzyme activity, altering tissue levels of carnosine, which in turn influences susceptibility to disorders such as diabetic nephropathy and cancer. Lower CNDP1 expression has been correlated with poorer prognosis in several tumor types, highlighting its potential utility as a prognostic biomarker. CNDP1’s structural activity depends on Zn^2+ as a cofactor and is regulated both genetically and posttranslationally. Although modulation of CNDP1 is being studied as a potential therapeutic approach, no approved drugs specifically targeting CNDP1 are currently available.

Other names

Beta-Ala-His dipeptidaseCN1CPGL2HsT2308Carnosinase 1Glutamate carboxypeptidase-like protein 2Serum carnosinaseHuman carnosinase

N/A (no approved drugs; hypothetical mechanisms include inhibition of dipeptidase activity to increase carnosine levels in tissues, which may modulate oxidative stress and inflammation, relevant in diabetic nephropathy and cancer)