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Literature summary extracted from

  • Zhao, L.; Liao, H; Tsai, M.D.
    The catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad in phosphatidylinositol-specific phospholipase C can be substituted by a chloride-ion (2004), J. Biol. Chem., 279, 31995-32000.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.13 wild-type and D274N mutant PI-PLC Bacillus thuringiensis

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.13 D274A catalytic aspartate mutation, 0.005% of wild-type activity, no activation by exogenous anions Bacillus thuringiensis
4.6.1.13 D274E catalytic aspartate mutation, 50% of wild-type activity, no activation by chloride ions Bacillus thuringiensis
4.6.1.13 D274G catalytic aspartate mutation, activation of mutant PI-PLC by exogenous anions, e.g. Cl- Bacillus thuringiensis
4.6.1.13 D274N catalytic aspartate mutation, 40fold decreased activity compared with wild-type enzyme, no activation by chloride ions Bacillus thuringiensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.13 additional information
-
 additional information kinetic data Bacillus thuringiensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.13 Cl- 1 M, 2-3fold activation of wild-type PI-PLC Bacillus thuringiensis

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.13 Bacillus thuringiensis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.13 wild-type and mutant PI-PLC Bacillus thuringiensis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.6.1.13 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol mechanism Bacillus thuringiensis
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.6.1.13 additional information
-
-
 Bacillus thuringiensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.13 1-phosphatidyl-1D-myo-inositol catalyzes the cleavage of the phosphorus-oxygen bond in phosphatidylinositol, catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad, catalytic mechanism, active site structure Bacillus thuringiensis 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.13 6 9 wild-type PI-PLC, in the absence of 1 M Cl- Bacillus thuringiensis
4.6.1.13 7 8 wild-type PI-PLC, in the presence of 1 M Cl- Bacillus thuringiensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.6.1.13 additional information
-
 pH-dependence study of wild-type and mutant PI-PLC Bacillus thuringiensis