Diphosphoinositol-polyphosphate diphosphatase

From Wikipedia, the free encyclopedia

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.

[edit] Structural studies

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

[edit] References

• IUBMB entry for 3.6.1.52
• BRENDA references for 3.6.1.52 (Recommended.)
• PubMed references for 3.6.1.52
• PubMed Central references for 3.6.1.52
• Google Scholar references for 3.6.1.52
• Shears SB (1998). "A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase". EMBO. J. 17: 6599–607. doi:10.1093/emboj/17.22.6599. 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: 12730–6. doi:10.1074/jbc.275.17.12730. PMID 10777568. 

[edit] External links

• IUBMB entry for 3.6.1.52

• KEGG entry for 3.6.1.52

• BRENDA entry for 3.6.1.52

• NiceZyme view of 3.6.1.52

• EC2PDB: PDB structures for 3.6.1.52

• PRIAM entry for 3.6.1.52

• PUMA2 entry for 3.6.1.52

• IntEnz: Integrated Enzyme entry for 3.6.1.52

• MetaCyc entry for 3.6.1.52

• Atomic-resolution structures of enzymes belonging to this class