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Literature summary extracted from

  • Feng, J.; Bradley, W.D.; Roberts, M.F.
    Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C (2003), J. Biol. Chem., 278, 24651-24657.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.13 diheptanoyl phosphatidylcholine activates Bacillus thuringiensis
4.6.1.13 Isopropanol water-miscible, 30%, activates Bacillus thuringiensis
4.6.1.13 phosphatidylcholine PI-PLC is activated by nonsubstrate interfaces such as phosphatidylcholine micelles or bilayers, activation corresponds with partial insertion into the interface of Trp-47 and Trp-242 in the rim of the alphabeta-barrel Bacillus thuringiensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.13 overexpression in Escherichia coli BL21 Bacillus thuringiensis

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.13 G238W study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 G238W/W242A double mutant with enhanced activation and affinity for phosphatidylcholine interfaces above that of wild-type PI-PLC Bacillus thuringiensis
4.6.1.13 G48W/W47A double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 I43W/W47A double mutant with recovered kinetic interfacial activation, lower specific activity than wild-type PI-PLC Bacillus thuringiensis
4.6.1.13 M49W/W47A double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 additional information tryptophan rescue mutagenesis, reinsertion of a Trp at a different place in helix B in the W47A mutant or in the loop of the W242A mutant Bacillus thuringiensis
4.6.1.13 N243W/W242A double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 Q45W/W47A double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 S236W/W242A double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol Bacillus thuringiensis
4.6.1.13 W242A mutant with much weaker binding to interfaces and lower kinetic interfacial activation Bacillus thuringiensis
4.6.1.13 W47A mutant with much weaker binding to interfaces and lower kinetic interfacial activation Bacillus thuringiensis

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
4.6.1.13 isopropanol water-miscible, 30%, activates 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 recombinant PI-PLC Bacillus thuringiensis

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 the active site is located at the C-terminal side Bacillus thuringiensis 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.13 54.4
-
 Tm-value, wild-type PI-PLC Bacillus thuringiensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.13 7
-
 assay at Bacillus thuringiensis