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Literature summary extracted from

  • Sharom, F.J.; Lehto, M.T.
    Glycosylphosphatidylinositol-anchored proteins: structure, function, and cleavage by phosphatidylinositol-specific phospholipase C (2002), Biochem. Cell Biol., 80, 535-549.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.4.11 additional information cleavage of GPI-anchored proteins by PI-PLC is influenced by bilayer fluidity, higher fluidity activates Bacillus thuringiensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.4.11
-
 Listeria monocytogenes
3.1.4.11 free form, in complex with myo-inositol and with glucosaminyl(alpha1-6)-D-myo-inositol Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.11 additional information
-
 additional information kinetic study of 5’-nucleotidase cleavage Bacillus thuringiensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.11 Bacillus cereus
-
-
-
3.1.4.11 Bacillus thuringiensis
-
-
-
3.1.4.11 Clostridium novyi
-
-
-
3.1.4.11 Listeria monocytogenes
-
-
-
3.1.4.11 Staphylococcus aureus
-
-
-

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 Bacillus cereus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.11 glycosylphosphatidylinositol + H2O catalytic mechanism Bacillus cereus ?
-
 ?
3.1.4.11 additional information PI-PLC has a high affinity for the glycosylphosphatidylinositol anchor of GPI-anchored proteins, e.g. 5’-nucleotidase and alkaline phosphatase, and catalyzes cleavage in vitro to release a soluble protein and diacylglycerol, which remains in the membrane Staphylococcus aureus ?
-
 ?
3.1.4.11 additional information PI-PLC has a high affinity for the glycosylphosphatidylinositol anchor of GPI-anchored proteins, e.g. 5’-nucleotidase and alkaline phosphatase, and catalyzes cleavage in vitro to release a soluble protein and diacylglycerol, which remains in the membrane Bacillus thuringiensis ?
-
 ?
3.1.4.11 additional information PI-PLC has a high affinity for the glycosylphosphatidylinositol anchor of GPI-anchored proteins, e.g. 5’-nucleotidase and alkaline phosphatase, and catalyzes cleavage in vitro to release a soluble protein and diacylglycerol, which remains in the membrane Clostridium novyi ?
-
 ?
3.1.4.11 additional information PI-PLC has a high affinity for the glycosylphosphatidylinositol anchor of GPI-anchored proteins, e.g. 5’-nucleotidase and alkaline phosphatase, and catalyzes cleavage in vitro to release a soluble protein and diacylglycerol, which remains in the membrane, enzyme structure Bacillus cereus ?
-
 ?
3.1.4.11 phosphatidylinositol + H2O phosphatidylinositol-specific, catalytic mechanism Bacillus cereus diacylglycerol + myo-inositol 1-phosphate
-
 ?