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{{Infobox enzyme
{{Infobox enzyme
| Name = Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
| Name = Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
| EC_number = 3.1.3.78
| EC_number = 3.1.3.78
| CAS_number =
| CAS_number =
| GO_code =
| IUBMB_EC_number = 3/1/3/78
| GO_code =
| image =
| image =
| width =
| width =
| caption =
| caption =
}}
}}
'''Phosphatidylinositol-4,5-bisphosphate 4-phosphatase''' ({{EC number|3.1.3.78}}, ''phosphatidylinositol-4,5-bisphosphate 4-phosphatase I'', ''phosphatidylinositol-4,5-bisphosphate 4-phosphatase II'', ''type I PtdIns-4,5-P2 4-Ptase'', ''type II PtdIns-4,5-P2 4-Ptase'', ''IpgD'', ''PtdIns-4,5-P2 4-phosphatase type I'', ''PtdIns-4,5-P2 4-phosphatase type II'', ''type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase'', ''type 1 4-phosphatase'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 4-phosphohydrolase''.<ref>{{cite journal | vauthors = Niebuhr K, Giuriato S, Pedron T, Philpott DJ, Gaits F, Sable J, Sheetz MP, Parsot C, Sansonetti PJ, Payrastre B | title = Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology | journal = The EMBO Journal | volume = 21 | issue = 19 | pages = 5069–78 | date = October 2002 | pmid = 12356723 | pmc = 129044 | doi = 10.1093/emboj/cdf522 }}</ref><ref>{{cite journal | vauthors = Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW | title = The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 52 | pages = 18854–9 | date = December 2005 | pmid = 16365287 | pmc = 1323219 | doi = 10.1073/pnas.0509740102 }}</ref><ref>{{cite journal | vauthors = Zou J, Marjanovic J, Kisseleva MV, Wilson M, Majerus PW | title = Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 43 | pages = 16834–9 | date = October 2007 | pmid = 17940011 | pmc = 2040409 | doi = 10.1073/pnas.0708189104 }}</ref><ref>{{cite journal | vauthors = Mason D, Mallo GV, Terebiznik MR, Payrastre B, Finlay BB, Brumell JH, Rameh L, Grinstein S | title = Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase | journal = The Journal of General Physiology | volume = 129 | issue = 4 | pages = 267–83 | date = April 2007 | pmid = 17389247 | pmc = 2151621 | doi = 10.1085/jgp.200609656 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''Phosphatidylinositol-4,5-bisphosphate 4-phosphatase''' (EC 3.1.3.78, '''phosphatidylinositol-4,5-bisphosphate 4-phosphatase I, phosphatidylinositol-4,5-bisphosphate 4-phosphatase II, type I PtdIns-4,5-P<sub>2</sub> 4-Ptase, type II PtdIns-4,5-P<sub>2</sub> 4-Ptase, IpgD, PtdIns-4,5-P<sub>2</sub> 4-phosphatase type I, PtdIns-4,5-P<sub>2</sub> 4-phosphatase type II, type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase, type 1 4-phosphatase''') is an [[enzyme]] with [[List of enzymes|systematic name]] '''1-phosphatidyl-1<small>D</small>-''myo''-inositol-4,5-bisphosphate 4-phosphohydrolase'''.<ref>{{cite journal | vauthors = Niebuhr K, Giuriato S, Pedron T, Philpott DJ, Gaits F, Sable J, Sheetz MP, Parsot C, Sansonetti PJ, Payrastre B | title = Conversion of PtdIns(4,5)P<sub>2</sub> into PtdIns(5)P by the ''S.flexneri'' effector IpgD reorganizes host cell morphology | journal = The EMBO Journal | volume = 21 | issue = 19 | pages = 5069–78 | date = October 2002 | pmid = 12356723 | pmc = 129044 | doi = 10.1093/emboj/cdf522 }}</ref><ref>{{cite journal | vauthors = Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW | title = The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 52 | pages = 18854–9 | date = December 2005 | pmid = 16365287 | pmc = 1323219 | doi = 10.1073/pnas.0509740102 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Zou J, Marjanovic J, Kisseleva MV, Wilson M, Majerus PW | title = Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 43 | pages = 16834–9 | date = October 2007 | pmid = 17940011 | pmc = 2040409 | doi = 10.1073/pnas.0708189104 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mason D, Mallo GV, Terebiznik MR, Payrastre B, Finlay BB, Brumell JH, Rameh L, Grinstein S | title = Alteration of epithelial structure and function associated with PtdIns(4,5)P<sub>2</sub> degradation by a bacterial phosphatase | journal = The Journal of General Physiology | volume = 129 | issue = 4 | pages = 267–83 | date = April 2007 | pmid = 17389247 | pmc = 2151621 | doi = 10.1085/jgp.200609656 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]


: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> 1-phosphatidyl-1D-myo-inositol 5-phosphate + [[phosphate]]
: 1-phosphatidyl-1<small>D</small>-''myo''-inositol 4,5-bisphosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> 1-phosphatidyl-1<small>D</small>-''myo''-inositol 5-phosphate + [[phosphate]]


This enzyme participates in one of the [[mammalian]] pathways for degradation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P2].
This enzyme participates in one of the [[mammalian]] pathways for degradation of 1-phosphatidyl-1<small>D</small>-''myo''-inositol 4,5-bisphosphate [PtdIns(4,5)P<sub>2</sub>].


== References ==
== References ==
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{{Esterases}}
{{Esterases}}
{{Enzymes}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
{{Portal bar|Biology|border=no}}


[[Category:EC 3.1.3]]
[[Category:EC 3.1.3]]

Latest revision as of 15:23, 26 August 2023

Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
Identifiers
EC no.3.1.3.78
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Phosphatidylinositol-4,5-bisphosphate 4-phosphatase (EC 3.1.3.78, phosphatidylinositol-4,5-bisphosphate 4-phosphatase I, phosphatidylinositol-4,5-bisphosphate 4-phosphatase II, type I PtdIns-4,5-P2 4-Ptase, type II PtdIns-4,5-P2 4-Ptase, IpgD, PtdIns-4,5-P2 4-phosphatase type I, PtdIns-4,5-P2 4-phosphatase type II, type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase, type 1 4-phosphatase) is an enzyme with systematic name 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 4-phosphohydrolase.[1][2][3][4] This enzyme catalyses the following chemical reaction

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

This enzyme participates in one of the mammalian pathways for degradation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P2].

References

[edit]
  1. ^ Niebuhr K, Giuriato S, Pedron T, Philpott DJ, Gaits F, Sable J, Sheetz MP, Parsot C, Sansonetti PJ, Payrastre B (October 2002). "Conversion of PtdIns(4,5)P2 into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology". The EMBO Journal. 21 (19): 5069–78. doi:10.1093/emboj/cdf522. PMC 129044. PMID 12356723.
  2. ^ Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW (December 2005). "The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases". Proceedings of the National Academy of Sciences of the United States of America. 102 (52): 18854–9. doi:10.1073/pnas.0509740102. PMC 1323219. PMID 16365287.
  3. ^ Zou J, Marjanovic J, Kisseleva MV, Wilson M, Majerus PW (October 2007). "Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis". Proceedings of the National Academy of Sciences of the United States of America. 104 (43): 16834–9. doi:10.1073/pnas.0708189104. PMC 2040409. PMID 17940011.
  4. ^ Mason D, Mallo GV, Terebiznik MR, Payrastre B, Finlay BB, Brumell JH, Rameh L, Grinstein S (April 2007). "Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase". The Journal of General Physiology. 129 (4): 267–83. doi:10.1085/jgp.200609656. PMC 2151621. PMID 17389247.
[edit]
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