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Literature summary for 4.6.1.13 extracted from

  • Feng, J.; Wehbi, H.; Roberts, M.F.
    Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C (2002), J. Biol. Chem., 277, 19867-19875.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Isopropanol 30%, activates Bacillus thuringiensis
additional information PI-PLC exhibits several types of kinetic interfacial activation by interfaces, roles of Trp-47 and Trp-242 Bacillus thuringiensis
phosphatidylcholine activates Bacillus thuringiensis

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
W178A mutant with reduced stability and specific activity, study of kinetic activation by micellar phosphatidylcholine Bacillus thuringiensis
W242A active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine Bacillus thuringiensis
W242F kinetic analysis, binding studies to phosphatidylcholine vesicles Bacillus thuringiensis
W242I kinetic analysis, binding studies to phosphatidylcholine vesicles Bacillus thuringiensis
W280A mutant with reduced stability, study of kinetic activation by micellar phosphatidylcholine Bacillus thuringiensis
W47A active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine Bacillus thuringiensis
W47A/W242A double mutant, no affinity for phospholipid surfaces, no kinetic activation by micellar phosphatidylcholine Bacillus thuringiensis
W47F kinetic analysis, binding studies to phosphatidylcholine vesicles Bacillus thuringiensis
W47I kinetic analysis, binding studies to phosphatidylcholine vesicles Bacillus thuringiensis

Inhibitors

Inhibitors Comment Organism Structure
myo-inositol poor competitive inhibitor Bacillus thuringiensis

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm recombinant PI-PLC, expressed in Escherichia coli BL21 Bacillus thuringiensis 5737
-

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
specific activities of wild-type and mutant PI-PLCs towards 1D-myo-inositol 1,2-cyclic phosphate in the absence and presence of different activators Bacillus thuringiensis
401
-
W47I mutant PI-PLC, phosphotransferase activity Bacillus thuringiensis
556
-
wild-type PI-PLC, phosphotransferase activity Bacillus thuringiensis
558
-
W47F mutant PI-PLC, phosphotransferase activity Bacillus thuringiensis
658
-
W242F mutant PI-PLC, phosphotransferase activity Bacillus thuringiensis
684
-
W242I mutant PI-PLC, phosphotransferase activity Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol Trp-47 and Trp-242 residues are important for enzyme to bind to interfaces, both activating zwitterionic and substrate anionic surfaces, micellar phosphatidylinositol is a better substrate than monomeric phosphatidylinositol Bacillus thuringiensis 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol a cyclic phosphodiesterase activity of PI-PLC converts 1D-myo-inositol 1,2-cyclic phosphate to inositol 1-phosphate ?
additional information not: phosphatidylcholine Bacillus thuringiensis ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
41.5
-
Tm-value, pH 8, W178A mutant PI-PLC Bacillus thuringiensis
47
-
Tm-value, pH 8, W280A mutant PI-PLC Bacillus thuringiensis
53.6
-
Tm-value, pH 8, W47A mutant PI-PLC Bacillus thuringiensis
54.4
-
Tm-value, pH 8, wild-type PI-PLC Bacillus thuringiensis
54.6
-
Tm-value, pH 8, W47A/W242A double mutant PI-PLC Bacillus thuringiensis
56.2
-
Tm-value, pH 8, W242A mutant PI-PLC Bacillus thuringiensis