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.^[1]^[2]^[3]^[4] 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 [PtdIns(4,5)P2].

References

↑ Niebuhr, K.; Giuriato, S.; Pedron, T.; Philpott, D.J.; Gaits, F.; Sable, J.; Sheetz, M.P.; Parsot, C.; Sansonetti, P.J.; Payrastre, B. (2002). "Conversion of PtdIns(4,5)P₂ into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology". EMBO J. 21 (19): 5069–5078. doi:10.1093/emboj/cdf522. PMC 129044. PMID 12356723.
↑ Ungewickell, A.; Hugge, C.; Kisseleva, M.; Chang, S.C.; Zou, J.; Feng, Y.; Galyov, E.E.; Wilson, M.; Majerus, P.W. (2005). "The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases". Proc. Natl. Acad. Sci. USA. 102 (52): 18854–18859. doi:10.1073/pnas.0509740102. PMID 16365287.
↑ Zou, J.; Marjanovic, J.; Kisseleva, M.V.; Wilson, M.; Majerus, P.W. (2007). "Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis". Proc. Natl. Acad. Sci. USA. 104 (43): 16834–16839. doi:10.1073/pnas.0708189104. PMID 17940011.
↑ Mason, D.; Mallo, G.V.; Terebiznik, M.R.; Payrastre, B.; Finlay, B.B.; Brumell, J.H.; Rameh, L.; Grinstein, S. (2007). "Alteration of epithelial structure and function associated with PtdIns(4,5)P₂ degradation by a bacterial phosphatase". J. Gen. Physiol. 129 (4): 267–283. doi:10.1085/jgp.200609656. PMID 17389247.

External links

Phosphatidylinositol-4,5-bisphosphate 4-phosphatase at the US 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 UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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