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Literature summary extracted from

  • Pu, M.; Roberts, M.F.; Gershenson, A.
    Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding (2009), Biochemistry, 48, 6835-6845.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.13 additional information for small unilamellar vesicles containing anionic lipids and phosphatidylcholine, PI-PLC binding is strengthened by even small amounts of phosphatidylcholine Bacillus thuringiensis

Application

EC Number Application Comment Organism
4.6.1.13 additional information optimization of PI-PLC binding to substrate-containing vesicles is a balancing act between anchoring the protein in the correct conformation and orientation while also allowing it to dissociate in order to find substrate phospholipids or GPI-anchored proteins by scooting and/or hopping Bacillus thuringiensis

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.13 H32A active site mutant, but binds to pure phosphatidylglycerol and pure phosphatidylcholine small unilamellar vesicles with essentially the same affinities as mutant N168C Bacillus thuringiensis
4.6.1.13 K44A 0.98% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles Bacillus thuringiensis
4.6.1.13 K44E 0.44% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles Bacillus thuringiensis
4.6.1.13 N168C 1% relative activity Bacillus thuringiensis
4.6.1.13 P42G 0.7% relative activity Bacillus thuringiensis
4.6.1.13 P42G impaired phosphatidylcholine binding, but still binds most tightly to mixed lipid vesicles Bacillus thuringiensis
4.6.1.13 Y246S/Y247S/Y248S/N168C impaired phosphatidylcholine binding, but still binds most tightly to mixed lipid vesicles. Has similar affinities for pure phosphatidylglycerol vesicles than mutant N168C, while the apparent Kd of for pure phosphatidylcholine vesicles is ca. 3 orders of magnitude higher than that of mutant N168C. Apparent Kd toward small unilamellar vesicles is about 1000fold higher than that of mutant N168C Bacillus thuringiensis
4.6.1.13 Y88A 2.92% relative activity, mutation near the lipid binding region. Is an extremely active enzyme whose specific activity is 3fold higher than recombinant PI-PLC, binds more weakly to small unilamellar vesicles than wild-type 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
-
 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 1630
-
 wild-type, for phosphatidylinositol/diC7-phosphatidylcholine, in 50 mM HEPES buffer, pH 7.5, with 1 mM EDTA, 5 mM dithiothreitol, and 0.1 mg/ml bovine serum albumin, at 28°C Bacillus thuringiensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.13 additional information Lys44 mediates the initial electrostatic interaction of the protein with substrate Bacillus thuringiensis ?
-
 ?
4.6.1.13 phosphatidylinositol
-
 Bacillus thuringiensis diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.13 phosphatidylinositol-specific phospholipase C
-
 Bacillus thuringiensis
4.6.1.13 PI-PLC
-
 Bacillus thuringiensis

General Information

EC Number General Information Comment Organism
4.6.1.13 physiological function for highly anionic membranes, but not phosphatidylcholine-rich vesicles, binding correlates well with relative activity Bacillus thuringiensis