Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.6.1.13 extracted from

  • Wehbi, H.; Feng, J.; Roberts, M.F.
    Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity (2003), Biochim. Biophys. Acta, 1613, 15-27.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dimethylformamide water-miscible, enhances phosphotransferase activity Bacillus thuringiensis
Dimethylsulfoxide water-miscible, enhances phosphotransferase activity Bacillus thuringiensis
Isopropanol water-miscible, maximum activation at 30%, activates regardless of the type of phosphatidylinositol substrate, enhances phosphotransferase activity Bacillus thuringiensis
additional information isopropanol and diheptanoylphosphatidylcholine activate the hydrolytic activity towards 1D-myo-inositol 1,2-cyclic phosphate, PI-PLC exhibits kinetic interfacial activation Bacillus thuringiensis
phosphatidylcholine activates Bacillus thuringiensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli MM294 Bacillus thuringiensis

General Stability

General Stability Organism
myo-inositol stabilizes Bacillus thuringiensis

Inhibitors

Inhibitors Comment Organism Structure
myo-inositol weak Bacillus thuringiensis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Ca2+-independent Bacillus thuringiensis

Organic Solvent Stability

Organic Solvent Comment Organism
isopropanol water/isopropanol mixture decreases stability, at 4°C protein secondary structure is stable for at least 1 week in 30% isopropanol, Tm-value for PI-PLC thermal denaturation decreases linearly with added isopropanol, in presence of 30% isopropanol the Tm-value decreases from 53.6 to 30°C, myo-inositol enhances thermostability in isopropanol Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant PI-PLC Bacillus thuringiensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
phosphotransferase activity towards phosphatidylinositol in several aggregation states in the absence and presence of 30% isopropanol Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol aggregated substrate is preferred over monomeric substrate 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
25
-
some thermal unfolding of PI-PLC occurs Bacillus thuringiensis
30
-
Tm-value in presence of 30% isopropanol, myo-inositol enhances thermostability in isopropanol Bacillus thuringiensis
53.6
-
Tm-value in absence of 30% isopropanol Bacillus thuringiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Bacillus thuringiensis