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Literature summary extracted from

  • Rhee, S.G.
    Regulation of phosphoinositide-specific phospholipase C (2001), Annu. Rev. Biochem., 70, 281-312.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.4.11 B cell antigen receptor induces activation of PLC-gamma2, pathway Mammalia
3.1.4.11 G protein alpha12 activates PLC-epsilon Homo sapiens
3.1.4.11 G protein betagamma activates PLC-beta isoenzymes with the exception of PLC-beta4 Mammalia
3.1.4.11 G protein qalpha activates PLC-beta isoenzymes, G protein-coupled receptor-mediated activation Mammalia
3.1.4.11 additional information modes of activation/activation pathways of the PLC isoenzymes beta, gamma, delta and epsilon Mammalia
3.1.4.11 Ras activator of PLC-epsilon Homo sapiens
3.1.4.11 receptor protein tyrosine kinase activates PLC-gamma, growth factor receptor-mediated activation Mammalia
3.1.4.11 T cell antigen receptor induces activation of PLC-gamma1, pathway Mammalia

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.11 PLC-delta1 complexed with inositol 1,4,5-trisphosphate Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.11 cell membrane the PH domain of PLC-delta1 may tether the enzyme to the cell membrane by specific binding to phosphatidylinositol 4,5-bisphosphate Rattus norvegicus
-
-
3.1.4.11 membrane PLC-beta Mammalia 16020
-
3.1.4.11 nucleus PLC-beta1 is the major isoform of the nucleus Mammalia 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.11 Ca2+ requirement, PLC isoenzymes beta, gamma, delta and epsilon, delta-type isoenzymes are most sensitive Mammalia
3.1.4.11 Ca2+ requirement, mode of Ca2+ binding at the catalytic domain of PLC-delta1 Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.11 85000
-
 x * 85000, about, PLC-delta isoenzymes, x * 120000-155000, PLC-beta and -gamma isoenzymes, x * 230000-260000, PLC-epsilon Mammalia
3.1.4.11 230000
-
 x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms Homo sapiens
3.1.4.11 260000
-
 x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O Mammalia regulation of PLC isoenzymes, cellular signaling 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol intracellular messengers ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.11 Homo sapiens
-
 PLC-epsilon
-
3.1.4.11 Mammalia
-
 PLC-beta, -gamma, -delta and -epsilon
-
3.1.4.11 Rattus norvegicus
-
 PLC-delta1
-
3.1.4.11 Rattus norvegicus PLC-delta1
-
 PLC-delta1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.11 phosphoprotein PLC-gamma1 and 2, tyrosine phosphorylation activates enzyme Mammalia

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol mechanism Mammalia
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.11 heart PLC-epsilon, most abundantly in Homo sapiens
-
3.1.4.11 additional information the two alternatively spliced forms of PLC-epsilon are present in a wide variety of human tissues Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O domain organization of the PLC isoenzymes beta, gamma, delta and epsilon, distinct regulatory domains Mammalia 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
-
 ?
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O domain structure of PLC-epsilon, contains RasGEF and RA domains Homo sapiens 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
-
 ?
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O PLC-delta1, structure of the catalytic domain, His-311 and His-356 act as general acid-base catalysts Rattus norvegicus 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol 4- and 5-phosphoryl groups of inositol 1,4,5-trisphosphate interact with the side chains of Lys-32 and Lys-57 and with those of Lys-30, Arg-40 and Lys-57 of PLC-delta1, respectively ?
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O regulation of PLC isoenzymes, cellular signaling Mammalia 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol intracellular messengers ?
3.1.4.11 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O PLC-delta1, structure of the catalytic domain, His-311 and His-356 act as general acid-base catalysts Rattus norvegicus PLC-delta1 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol 4- and 5-phosphoryl groups of inositol 1,4,5-trisphosphate interact with the side chains of Lys-32 and Lys-57 and with those of Lys-30, Arg-40 and Lys-57 of PLC-delta1, respectively ?
3.1.4.11 phosphatidylinositol + H2O PLC-delta1, structure of the catalytic domain Rattus norvegicus ?
-
 ?
3.1.4.11 phosphatidylinositol + H2O PLC-delta1, structure of the catalytic domain Rattus norvegicus PLC-delta1 ?
-
 ?
3.1.4.11 phosphatidylinositol 4-phosphate + H2O PLC-delta1, structure of the catalytic domain Rattus norvegicus ?
-
 ?
3.1.4.11 phosphatidylinositol 4-phosphate + H2O PLC-delta1, structure of the catalytic domain Rattus norvegicus PLC-delta1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.11 ? x * 85000, about, PLC-delta isoenzymes, x * 120000-155000, PLC-beta and -gamma isoenzymes, x * 230000-260000, PLC-epsilon Mammalia
3.1.4.11 ? x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.1.4.11 additional information four PLC subfamilies: beta, gamma, delta and epsilon Mammalia