From Wikipedia, the free encyclopedia
phosphoinositide 5-phosphatase
Identifiers
EC no. 3.1.3.36
CAS no. 9036-01-5
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme phosphoinositide 5-phosphatase (EC 3.1.3.36) catalyzes the reaction

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase. Other names in common use include type II inositol polyphosphate 5-phosphatase, triphosphoinositide phosphatase, IP3 phosphatase, PtdIns(4,5)P2 phosphatase, triphosphoinositide phosphomonoesterase, diphosphoinositide phosphatase, inositol 1,4,5-triphosphate 5-phosphomonoesterase, inositol triphosphate 5-phosphomonoesterase, phosphatidylinositol-bisphosphatase, phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase, phosphatidylinositol 4,5-bisphosphate phosphatase, polyphosphoinositol lipid 5-phosphatase, and phosphatidyl-inositol-bisphosphate phosphatase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1UFW, 1W80, 2DNR, and 2QV2.

References

  • Dawson RM, Thompson W (1964). "The triphosphoinositide phosphomonoesterase of brain tissue". Biochem. J. 91 (2): 244–50. doi: 10.1042/bj0910244. PMC  1202879. PMID  4284485.
  • Roach PD, Palmer FB (1981). "Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase". Biochim. Biophys. Acta. 661 (2): 323–33. doi: 10.1016/0005-2744(81)90021-8. PMID  6271223.
  • Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, p. 320-338.


From Wikipedia, the free encyclopedia
phosphoinositide 5-phosphatase
Identifiers
EC no. 3.1.3.36
CAS no. 9036-01-5
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme phosphoinositide 5-phosphatase (EC 3.1.3.36) catalyzes the reaction

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase. Other names in common use include type II inositol polyphosphate 5-phosphatase, triphosphoinositide phosphatase, IP3 phosphatase, PtdIns(4,5)P2 phosphatase, triphosphoinositide phosphomonoesterase, diphosphoinositide phosphatase, inositol 1,4,5-triphosphate 5-phosphomonoesterase, inositol triphosphate 5-phosphomonoesterase, phosphatidylinositol-bisphosphatase, phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase, phosphatidylinositol 4,5-bisphosphate phosphatase, polyphosphoinositol lipid 5-phosphatase, and phosphatidyl-inositol-bisphosphate phosphatase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1UFW, 1W80, 2DNR, and 2QV2.

References

  • Dawson RM, Thompson W (1964). "The triphosphoinositide phosphomonoesterase of brain tissue". Biochem. J. 91 (2): 244–50. doi: 10.1042/bj0910244. PMC  1202879. PMID  4284485.
  • Roach PD, Palmer FB (1981). "Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase". Biochim. Biophys. Acta. 661 (2): 323–33. doi: 10.1016/0005-2744(81)90021-8. PMID  6271223.
  • Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, p. 320-338.



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