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Literature summary for 4.6.1.13 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)

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

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Purification (Commentary)

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

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

pH Range

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