Diphosphoinositol-polyphosphate diphosphatase

Diphosphoinositol-polyphosphate diphosphatase
Identifiers
EC number	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
Search PMC articles PubMed articles

In enzymology, a diphosphoinositol-polyphosphate diphosphatase (EC 3.6.1.52) is an enzyme that catalyzes the chemical reaction

diphospho-myo-inositol polyphosphate + H₂O $\rightleftharpoons$ 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

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2DUK, 2FVV, and 2Q9P.

References

• Shears SB; 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171006. 
• 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. 

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