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Literature summary for 4.6.1.13 extracted from

  • Wehbi, H.; Feng, J.; Kolbeck, J.; Ananthanarayanan, B.; Cho, W.; Roberts, M.F.
    Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C (2003), Biochemistry, 42, 9374-9382.
    View publication on PubMed
Search for more literature for 4.6.1.13

Activating Compound

Activating Compound Comment Organism Structure
phosphatidic acid binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism Bacillus thuringiensis
phosphatidylcholine binding to nonsubstrate zwitterionic phosphatidylcholine interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism Bacillus thuringiensis
phosphatidylglycerol binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism Bacillus thuringiensis
phosphatidylmethanol binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism Bacillus thuringiensis
phosphatidylserine binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism Bacillus thuringiensis

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant PI-PLC, expression in Escherichia coli BL21 Bacillus thuringiensis

Protein Variants

Protein Variants Comment Organism
K44A interfacial binding study Bacillus thuringiensis
R69D active site mutant with low specific activity towards phosphatidylinositol, interfacial binding study Bacillus thuringiensis
W242A interfacial binding study Bacillus thuringiensis
W47A interfacial binding study Bacillus thuringiensis
W47A/W242A double mutant, interfacial binding study Bacillus thuringiensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant 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 general acid/general base mechanism Bacillus thuringiensis
a

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 general acid/general base mechanism, enhanced activity when phosphatidylinositol is present in an interface compared to monomeric substrate Bacillus thuringiensis 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol PI-PLC catalyzes the hydrolysis of myo-inositol 1,2-cyclic phosphate to myo-inositol 1-phosphate ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
 cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine Bacillus thuringiensis

pH Range

pH Minimum pH Maximum Comment Organism
8
-
 cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine, drop in activity around pH 8, consistent with the drop in binding affinity for activating surfaces Bacillus thuringiensis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus thuringiensis theoretical pI
-
 5.4