Diphosphoinositol-polyphosphate diphosphatase
| Diphosphoinositol-polyphosphate diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.52 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a diphosphoinositol-polyphosphate diphosphatase (EC 3.6.1.52) is an enzyme that catalyzes the chemical reaction
- diphospho-myo-inositol polyphosphate + H2O myo-inositol polyphosphate + phosphate
Thus, the two substrates of this enzyme are diphospho-myo-inositol polyphosphate and H2O, whereas its two products are myo-inositol polyphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is diphospho-myo-inositol-polyphosphate diphosphohydrolase. Other names in common use include diphosphoinositol-polyphosphate phosphohydrolase, and DIPP.
Structural studies
[edit]As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2DUK, 2FVV, and 2Q9P.
References
[edit]- Safrany, ST; Caffrey, JJ; Yang, X; Bembenek, ME; Moyer, MB; Burkhart, WA; Shears, SB (1998). "A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase". EMBO J. 17 (22): 6599–607. doi:10.1093/emboj/17.22.6599. PMC 1171006. PMID 9822604.
- Caffrey JJ, Safrany ST, Yang X, Shears SB (2000). "Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family". J. Biol. Chem. 275 (17): 12730–6. doi:10.1074/jbc.275.17.12730. PMID 10777568.
