Aminoacylhistidine dipeptidase

Aminoacylhistidine dipeptidase (also known as Carnosinase, CN1, or CN2) is an enzyme that catalyzes the hydrolysis of carnosine and other dipeptides. This enzyme is encoded by the CNDP1 and CNDP2 genes in humans.

Function

Aminoacylhistidine dipeptidase is a cytosolic, non-specific dipeptidase that cleaves a variety of dipeptides including carnosine and anserine. It is most active at neutral to slightly alkaline pH and requires one zinc ion per subunit for its activity.

Structure

The enzyme is a homodimer with each subunit consisting of a single polypeptide chain of about 500 amino acids. The active site of the enzyme contains a zinc ion, which is essential for its catalytic activity.

Clinical significance

Mutations in the CNDP1 gene have been associated with carnosinemia, a rare metabolic disorder characterized by an excess of carnosine in the urine. In addition, the enzyme has been implicated in the pathogenesis of diabetic nephropathy, a common complication of diabetes mellitus.

See also

• Carnosine
• Dipeptidase
• Carnosinemia
• Diabetic nephropathy