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.[1] ADPRP belongs to the family of NUDIX hydrolase.
Structural highlights
ADPRP contains two domains: the and the C-terminal which contains the active site. The C-terminal domain contains the which is typical to pyrophosphatases and binds the metal ion. .[2] Water molecules are shown as red spheres.
