BRENDA - Enzyme Database

Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C

Wehbi, H.; Feng, J.; Kolbeck, J.; Ananthanarayanan, B.; Cho, W.; Roberts, M.F.; Biochemistry 42, 9374-9382 (2003)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
Organism
4.6.1.13
wild-type and mutant PI-PLC, expression in Escherichia coli BL21
Bacillus thuringiensis
Engineering
EC Number
Amino acid exchange
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
4.6.1.13
Bacillus thuringiensis
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.6.1.13
recombinant wild-type and mutant PI-PLC
Bacillus thuringiensis
Reaction
EC Number
Reaction
Commentary
Organism
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
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.6.1.13
additional information
-
-
Bacillus thuringiensis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
650231
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
650231
Bacillus thuringiensis
?
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.6.1.13
7.1
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
Bacillus thuringiensis
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
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
Commentary
pI Value Maximum
pI Value
4.6.1.13
Bacillus thuringiensis
theoretical pI
-
5.4
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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) (protein specific)
EC Number
Commentary
Organism
4.6.1.13
wild-type and mutant PI-PLC, expression in Escherichia coli BL21
Bacillus thuringiensis
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.6.1.13
recombinant wild-type and mutant PI-PLC
Bacillus thuringiensis
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.6.1.13
additional information
-
-
Bacillus thuringiensis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
650231
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
650231
Bacillus thuringiensis
?
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.6.1.13
7.1
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
Bacillus thuringiensis
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
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 (protein specific)
EC Number
Organism
Commentary
pI Value Maximum
pI Value
4.6.1.13
Bacillus thuringiensis
theoretical pI
-
5.4