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

BRENDA support

Literature summary 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

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.13 K44A interfacial binding study Bacillus thuringiensis
4.6.1.13 R69D active site mutant with low specific activity towards phosphatidylinositol, interfacial binding study Bacillus thuringiensis
4.6.1.13 W242A interfacial binding study Bacillus thuringiensis
4.6.1.13 W47A interfacial binding study Bacillus thuringiensis
4.6.1.13 W47A/W242A double mutant, interfacial binding study 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 wild-type and mutant PI-PLC Bacillus thuringiensis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.6.1.13 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]

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 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.13 7.1
-
 cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine Bacillus thuringiensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.6.1.13 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

EC Number Organism Comment pI Value Maximum pI Value
4.6.1.13 Bacillus thuringiensis theoretical pI
-
 5.4