Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.78
Description:Phosphatidylinositol-4,5-bisphosphate 4-phosphatase.
Alternative Name: PtdIns-4,5-P(2) 4-phosphatase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.78
BRENDA Enzyme Link: BRENDA 3.1.3.78
KEGG Enzyme Link: KEGG3.1.3.78
BioCyc Enzyme Link: BioCyc 3.1.3.78
ExPASy Enzyme Link: ExPASy3.1.3.78
EC2PDB Enzyme Link: EC2PDB 3.1.3.78
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.78
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.78
IntEnz Enzyme Link: IntEnz 3.1.3.78
MEDLINE Enzyme Link: MEDLINE 3.1.3.78
MSA:

3.1.3.78;

Phylogenetic Tree:

3.1.3.78;

Uniprot:
M-CSA:
RHEA:25674 a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis.Zou J, Marjanovic J, Kisseleva MV, Wilson M, Majerus PW2007 Oct 2317940011
Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase.Mason D, Mallo GV, Terebiznik MR, Payrastre B, Finlay BB, Brumell JH, Rameh L, Grinstein S2007 Apr17389247
The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases.Ungewickell A, Hugge C, Kisseleva M, Chang SC, Zou J, Feng Y, Galyov EE, Wilson M, Majerus PW2005 Dec 2716365287
Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S.flexneri effector IpgD reorganizes host cell morphology.Niebuhr K, Giuriato S, Pedron T, Philpott DJ, Gaits F, Sable J, Sheetz MP, Parsot C, Sansonetti PJ, Payrastre B2002 Oct 112356723