ADP-ribose pyrophosphatase

Function

ADP-ribose pyrophosphatase (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.

Structural highlights

ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site.