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Literature summary for 3.1.4.11 extracted from

  • Leondaritis, G.; Sarri, T.; Dafnis, I.; Efstathiou, A.; Galanopoulou, D.
    Biochemical and genetic evidence for the presence of multiple phosphatidylinositol- and phosphatidylinositol 4,5-bisphosphate-specific phospholipases C in Tetrahymena (2011), Eukaryot. Cell, 10, 412-422.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
GTPgammaS one of the isozymes is activated by GTPgammaS in vitro Tetrahymena thermophila

Inhibitors

Inhibitors Comment Organism Structure
U73122 i.e. 1-(6-([17beta-3-methoxyestra-1,3,5(10)-trien-17-yl]amino)hexyl)-1H-pyrrole-2,5-dione, one of the isozymes is inhibited Tetrahymena thermophila

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane one of the isozymes is a membrane-associated PI-PLC Tetrahymena thermophila 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, one of the isozymes is activated by low-micromolar Ca2+ Tetrahymena thermophila

Organism

Organism UniProt Comment Textmining
Tetrahymena thermophila
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several strains, 4 genes encoding 1 bacterial type PI-PLC and 3 eukaryotic type PI-PLCs
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Synonyms

Synonyms Comment Organism
phosphoinositide-specific phospholipases C
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Tetrahymena thermophila
PI-PLC
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Tetrahymena thermophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Tetrahymena thermophila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Tetrahymena thermophila

General Information

General Information Comment Organism
malfunction inhibition of PI-PLC in vivo resultes in rapid upregulation of PtdIns(4,5)P2 levels Tetrahymena thermophila
physiological function PI-PLC shows functional importance in regulating phosphoinositide turnover in Tetrahymena. Eukaryotic PI-PLC specifically hydrolyzes phosphatidylinositol 4,5-bisphosphate to produce the Ca2+-mobilizing agent inositol 1,4,5-trisphosphate, and regulates signaling in multicellular organisms. Bacterial PtdIns-specific PLCs hydrolyze PtdIns and glycosyl-PtdIns, and are considered important virulence factors. Tetrahymena species are unique in that they contain two sets of functional genes coding for both 1 bacterial and 3 eukaryotic PLCs, one of which is inactive. Expression patterns and PI-PLC activities in three Tetrahymena thermophila strains showed a correlation between expression levels and activity, suggesting that the three eukaryotic PI-PLC genes are functionally nonredundant. The two PLC activities differ in their phosphoinositide substrate utilization, subcellular localization, secretion to extracellular space, and sensitivity to Ca2+ Tetrahymena thermophila