Carnosine Dipeptidase 2 (CNDP2)

CNDP2 is a nonspecific dipeptidase rather than a selective carnosinase.The deduced 473-amino acid protein has a calculated molecular mass of 52.9 kD. CN2 contains essential histidine and carboxyl residues in the metal-binding site, as well as 3 N-glycosylation sites. CN2 shares 49% amino acid identity with CN1 (CNDP1), but it lacks the N-terminal signal sequence found in CN1. mRNA dot blot analysis detected CN2 expression in all adult and fetal tissues examined. Western blot analysis detected widespread protein expression. Highest levels were in kidney and liver, with lower levels in brain, spleen, ovary, testis, lung, and pancreas. No protein expression was found in heart. Size-exclusion chromatography indicated that purified recombinant CN2 created a homodimer of 90 kD.