Phosphatidylinositol-4,5-bisphosphate 4-phosphatase

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. This enzyme catalyses the following chemical reaction

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

\rightleftharpoons

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 .

References

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.
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.
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.
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.

External links

Phosphatidylinositol-4,5-bisphosphate+4-phosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.1.3