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Literature summary for 4.6.1.13 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

Activating Compound Comment Organism Structure
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
dihexanoylphosphatidylcholine non-substrate activator lipid, maximum PI-PLC activity at 0.7-1 mM Bacillus cereus

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol mechanism Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol natural substrate Bacillus cereus 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
?
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
-
?
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
-
?
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

Subunits Comment Organism
monomer 1 * 35000 Bacillus cereus

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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