ADP-ribose pyrophosphatase

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Function

ADP-ribose pyrophosphatase (ADPRP) or ADPRase 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.

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3D structures of ADP-ribose pyrophosphatase

ADP-ribose pyrophosphatase 3D structures


ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, 1khz

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ReferencesReferences

  1. ↑ Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat Struct Biol. 2001 May;8(5):467-72. PMID:11323725 doi:10.1038/87647
  2. ↑ Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry. 2002 Jul 30;41(30):9279-85. PMID:12135348

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