| ADP-ribose diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.13 | ||||||||
| CAS no. | 9024-83-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
ADP-ribose diphosphatase (EC 3.6.1.13) is an enzyme that catalyzes a hydrolysis reaction in which water nucleophilically attacks ADP-ribose to produce AMP and D-ribose 5-phosphate. Enzyme hydrolysis occurs by the breakage of a phosphoanhydride bond and is dependent on Mg2+ ions that are held in complex by the enzyme.
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The C-terminal domain of ADP-ribose diphosphatase contains the Nudix sequence, a highly conserved amino acid sequence that is found in over 450 putative proteins in about 90 different species. A part of this sequence known as the Nudix fold is the catalytic part of the sequence. It is a structurally conserved loop-helix-loop motif that creates a scaffold for metal binding and pyrophosphatase chemistry in the enzyme.[1]
ADP-ribose hydrolases in general act as protective agents against excessive intracellular accumulation of ADP-ribose, as high intracellular levels of ADP-ribose can be damaging to the cell. ADP-ribose diphosphatase, in particular, hydrolyzes ADP-ribose into AMP and D-ribose 5-phosphate, both of which are intermediates of central metabolic pathways and therefore are easily reused.[2][3]
Other common names for ADP-ribose diphosphatase include ADP-ribose pyrophosphatase and ADPRase. ADP-ribose is commonly referred to as ADPR.
- ^ Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM (May 2001). "The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family". Nature Structural Biology. 8 (5): 467–72. doi:10.1038/87647. PMID 11323725. S2CID 10896410.
- ^ Galperin MY, Moroz OV, Wilson KS, Murzin AG (January 2006). "House cleaning, a part of good housekeeping". Molecular Microbiology. 59 (1): 5–19. doi:10.1111/j.1365-2958.2005.04950.x. PMID 16359314. S2CID 10313196.
- ^ Ribeiro JM, Carloto A, Costas MJ, Cameselle JC (April 2001). "Human placenta hydrolases active on free ADP-ribose: an ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase". Biochimica et Biophysica Acta (BBA) - General Subjects. 1526 (1): 86–94. doi:10.1016/S0304-4165(01)00113-1. PMID 11287126.