Activating Compound | Comment | Organism | Structure |
---|---|---|---|
GTPgammaS | one of the isozymes is activated by GTPgammaS in vitro | Tetrahymena thermophila |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | one of the isozymes is a membrane-associated PI-PLC | Tetrahymena thermophila | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required, one of the isozymes is activated by low-micromolar Ca2+ | Tetrahymena thermophila |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Tetrahymena thermophila | - |
several strains, 4 genes encoding 1 bacterial type PI-PLC and 3 eukaryotic type PI-PLCs | - |
Synonyms | Comment | Organism |
---|---|---|
phosphoinositide-specific phospholipases C | - |
Tetrahymena thermophila |
PI-PLC | - |
Tetrahymena thermophila |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Tetrahymena thermophila |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Tetrahymena thermophila |
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 |