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

BRENDA support

Literature summary extracted from

  • Birrell, G.B.; Zaikova, T.O.; Rukavishnikov, A.V.; Keana, J.F.W.; Griffith, O.H.
    Allosteric interactions within subsites of a monomeric enzyme: Kinetics of fluorogenic substrates of PI-specific phospholipase C (2003), Biophys. J., 84, 3264-3275.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.13 butyl-fluorescein myo-inositol phosphate two molecules bind to enzyme, one at the active site and one at a subsite, causing an increase in activity, kinetics Bacillus cereus
4.6.1.13 dihexanoylphosphatidylcholine non-substrate activator lipid, maximum PI-PLC activity at 0.7-1 mM Bacillus cereus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.13 additional information
-
 additional information kinetics of butyl-fluorescein myo-inositol phosphate and methyl-fluorescein myo-inositol phosphate cleavage, two-site kinetic model Bacillus cereus
4.6.1.13 0.14
-
 methyl-fluorescein myo-inositol phosphate pH 7, 25°C, in presence of dihexanoylphosphatidylcholine Bacillus cereus
4.6.1.13 0.81
-
 methyl-fluorescein myo-inositol phosphate pH 7, 25°C, in absence of dihexanoylphosphatidylcholine Bacillus cereus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.6.1.13 35000
-
 1 * 35000 Bacillus cereus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.6.1.13 1-phosphatidyl-1D-myo-inositol Bacillus cereus natural substrate 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.13 Bacillus cereus
-
-
-

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 mechanism Bacillus cereus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.13 1-phosphatidyl-1D-myo-inositol natural substrate Bacillus cereus 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
 ?
4.6.1.13 1-phosphatidyl-1D-myo-inositol cleaves phosphatidylinositol in a rapid intramolecular transphosphorylation reaction forming the products, in a second reaction the cyclic phosphorylase activity of PI-PLC catalyzes the slow hydrolysis of 1D-myo-inositol 1,2-cyclic phosphate to D-myo-inositol 1-phosphate, utilizes His-32 and His-82 in a general acid catalysis mechanism Bacillus cereus 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
 ?
4.6.1.13 butyl-fluorescein myo-inositol phosphate two substrate molecules bind to enzyme, one at the active site and one at a subsite, causing an increase in activity, subsite interactions of PI-PLC Bacillus cereus D-myo-inositol 1,2-cyclic phosphate + butyl-fluorescein
-
 ?
4.6.1.13 methyl-fluorescein myo-inositol phosphate substrate binds only to the active site and not to the activator site Bacillus cereus D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.13 monomer 1 * 35000 Bacillus cereus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.6.1.13 25
-
 assay at Bacillus cereus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6.1.13 additional information
-
 additional information
-
 Bacillus cereus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.13 7
-
 assay at Bacillus cereus