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Information on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase and Organism(s) Bacillus thuringiensis and UniProt Accession P08954
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4.6.1.13 phosphatidylinositol diacylglycerol-lyaseIUBMB Comments
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
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Word Map
- 4.6.1.13
- 11beta-hydroxysteroid
- cortisone
-
phosphatidylcholine-specific
- 11beta-hsd2
- pc-plc
- molecular biology
- analysis
- medicine
The taxonomic range for the selected organisms is: Bacillus thuringiensis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
phosphatidylinositol-specific plc, pi-phospholipase c, 1-phosphatidylinositol phosphodiesterase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphatidylinositol-specific phospholipase C
-
1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming)
-
-
-
-
1-phosphatidylinositol phosphodiesterase
-
-
-
-
monophosphatidylinositol phosphodiesterase
-
-
-
-
Phosphatidylinositol diacylglycerol-lyase
-
-
-
-
phosphatidylinositol phosphodiesterase
-
-
-
-
phosphatidylinositol phospholipase C
-
-
-
-
phosphatidylinositol-specific phospholipase C
phosphatidylinositol-specific phospholipase C
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
mechanism
-
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
general acid/general base mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-1,2-cyclic-phosphate-forming)
This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.
CAS REGISTRY NUMBER
COMMENTARY
37288-19-0
-
63551-76-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
aggregated substrate is preferred over monomeric substrate
a cyclic phosphodiesterase activity of PI-PLC converts 1D-myo-inositol 1,2-cyclic phosphate to inositol 1-phosphate
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
catalyzes the cleavage of the phosphorus-oxygen bond in phosphatidylinositol, catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad, catalytic mechanism, active site structure
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
general acid/general base mechanism, enhanced activity when phosphatidylinositol is present in an interface compared to monomeric substrate
PI-PLC catalyzes the hydrolysis of myo-inositol 1,2-cyclic phosphate to myo-inositol 1-phosphate
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
the active site is located at the C-terminal side
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
Trp-47 and Trp-242 residues are important for enzyme to bind to interfaces, both activating zwitterionic and substrate anionic surfaces, micellar phosphatidylinositol is a better substrate than monomeric phosphatidylinositol
a cyclic phosphodiesterase activity of PI-PLC converts 1D-myo-inositol 1,2-cyclic phosphate to inositol 1-phosphate
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
myo-inositol-1,2-cyclic phosphate appears as sole product
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
degrades synthetic phosphatidylinositols in the following order dilauroyl > dimyristoly > dioleoyl > dipalmitoyl. At first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action
-
-
?
additional information
?
-
-
approximately 20% of the alkaline phosphodiesterase I activity is released from the apical surface of the pig LLC-PK1 cells by the action of the 1-phosphatidylinositol phosphodiesterase
-
-
?
additional information
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
?
additional information
?
-
-
Lys44 mediates the initial electrostatic interaction of the protein with substrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
-
-
-
?
additional information
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethylformamide
-
water-miscible, enhances phosphotransferase activity
Dimethylsulfoxide
-
water-miscible, enhances phosphotransferase activity
phosphatidic acid
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylglycerol
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylmethanol
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylserine
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Isopropanol
-
water-miscible, maximum activation at 30%, activates regardless of the type of phosphatidylinositol substrate, enhances phosphotransferase activity
phosphatidylcholine
-
binding to nonsubstrate zwitterionic phosphatidylcholine interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylcholine
-
PI-PLC is activated by nonsubstrate interfaces such as phosphatidylcholine micelles or bilayers, activation corresponds with partial insertion into the interface of Trp-47 and Trp-242 in the rim of the alphabeta-barrel
additional information
-
isopropanol and diheptanoylphosphatidylcholine activate the hydrolytic activity towards 1D-myo-inositol 1,2-cyclic phosphate, PI-PLC exhibits kinetic interfacial activation
-
additional information
-
PI-PLC exhibits several types of kinetic interfacial activation by interfaces, roles of Trp-47 and Trp-242
-
additional information
-
for small unilamellar vesicles containing anionic lipids and phosphatidylcholine, PI-PLC binding is strengthened by even small amounts of phosphatidylcholine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.8
mutant Y246S/Y247S/Y248S/Y251S, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
1.6
mutant Y246S/Y247S/Y248S/Y251S, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
112
mutant Y246S/Y247S/Y248S/Y251S, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
2.1
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
2.9
mutant Y246S/Y247S/Y248S, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
239
mutant Y247S/Y251S, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
301
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
375
wild-type, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
41
mutant Y247S/Y251S, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
560
wild-type, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
6.7
mutant Y247S/Y251S, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
62
mutant Y246S/Y247S/Y248S/Y251S, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
670
mutant Y247S/Y251S, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
73
wild-type, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
9.5
wild-type, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
98
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
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
additional information
additional information
-
phosphotransferase activity towards phosphatidylinositol in several aggregation states in the absence and presence of 30% isopropanol
additional information
-
specific activities of wild-type and mutant PI-PLCs towards 1D-myo-inositol 1,2-cyclic phosphate in the absence and presence of different activators
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine, drop in activity around pH 8, consistent with the drop in binding affinity for activating surfaces
additional information
-
pH-dependence study of wild-type and mutant PI-PLC
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant PI-PLC, expressed in Escherichia coli BL21
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
for highly anionic membranes, but not phosphatidylcholine-rich vesicles, binding correlates well with relative activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
although small amounts of dimer have been noted previously
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant Y247S/Y251S in the absence and presence of myo-inositol as well as mutant Y246S/Y247S/Y248S/Y251S, both mutant proteins crystallize as monomers, are very similar to one another, and have no change in the active site region
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I43W/W47I
are made by introducing the second mutation in the gene coding for a single mutant
L39A/V46A
are made by introducing the second mutation in the gene coding for a single mutant
W47A/W242A
dimeric mutant, which is unable to bind to phosphatidycholine
Y246A/Y247A
the variant shows significant membrane binding defects
Y246S/Y247S/Y248S
less active toward phosphatidylinositol solubilized in diheptanoylphosphatidylcholine and when changing the detergent matrix to Triton X-100, as the wild-type
Y246S/Y247S/Y248S/Y251S
less active toward phosphatidylinositol solubilized in diheptanoylphosphatidylcholine and when changing the detergent matrix to Triton X-100, as the wild-type
Y247S/Y251S
exhibits specific activity toward phosphatidylinositol solubilized in diheptanoylphosphatidylcholine comparable to wild-type. Reduced specific activity, when changing the detergent matrix to Triton X-100
Y86A/Y88A
the mutations decrease membrane affinity for the enzyme
D274A
-
catalytic aspartate mutation, 0.005% of wild-type activity, no activation by exogenous anions
D274E
-
catalytic aspartate mutation, 50% of wild-type activity, no activation by chloride ions
D274G
-
catalytic aspartate mutation, activation of mutant PI-PLC by exogenous anions, e.g. Cl-
D274N
-
catalytic aspartate mutation, 40fold decreased activity compared with wild-type enzyme, no activation by chloride ions
G238W
-
study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
G238W/W242A
-
double mutant with enhanced activation and affinity for phosphatidylcholine interfaces above that of wild-type PI-PLC
G48W/W47A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
H32A
-
active site mutant, but binds to pure phosphatidylglycerol and pure phosphatidylcholine small unilamellar vesicles with essentially the same affinities as mutant N168C
I43W/W47A
-
double mutant with recovered kinetic interfacial activation, lower specific activity than wild-type PI-PLC
K44A
K44E
-
0.44% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles
M49W/W47A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
N243W/W242A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
P42G
Q45W/W47A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
R69D
-
active site mutant with low specific activity towards phosphatidylinositol, interfacial binding study
S236W/W242A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
W178A
-
mutant with reduced stability and specific activity, study of kinetic activation by micellar phosphatidylcholine
W242A
W242F
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
W242I
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
W280A
-
mutant with reduced stability, study of kinetic activation by micellar phosphatidylcholine
W47A
W47A/W242A
W47F
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
W47I
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
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
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
additional information
K44A
-
0.98% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles
P42G
-
impaired phosphatidylcholine binding, but still binds most tightly to mixed lipid vesicles
W242A
-
active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine
W242A
-
mutant with much weaker binding to interfaces and lower kinetic interfacial activation
W47A
-
active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine
W47A
-
mutant with much weaker binding to interfaces and lower kinetic interfacial activation
W47A/W242A
-
double mutant, no affinity for phospholipid surfaces, no kinetic activation by micellar phosphatidylcholine
additional information
replacing two tyrosines have small effects on enzyme activity. Removal of three or four tyrosine residues weakens binding to phosphatidylcholine surfaces and reduces phosphatidylinositol cleavage by the enzyme as well as phosphatidylcholine activation of inositol 1,2-(cyclic)-phosphate hydrolysis
additional information
-
tryptophan rescue mutagenesis, reinsertion of a Trp at a different place in helix B in the W47A mutant or in the loop of the W242A mutant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
Tm-value in presence of 30% isopropanol, myo-inositol enhances thermostability in isopropanol
53.6
54.4
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isopropanol
isopropanol
-
water/isopropanol mixture decreases stability, at 4°C protein secondary structure is stable for at least 1 week in 30% isopropanol, Tm-value for PI-PLC thermal denaturation decreases linearly with added isopropanol, in presence of 30% isopropanol the Tm-value decreases from 53.6 to 30°C, myo-inositol enhances thermostability in isopropanol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and phenyl Sepharose column chromatography
Q-sepharose fast-flow column and phenyl-Sepharose column, monitored by SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
transformed into Escherichia coli BL21-Codonplus (DE3)-RIL cells
expression in Escherichia coli, construction of four vectors for high-level expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of the enzyme and specific antibodies for the enzyme for the examination of the growth inhibition, morphological change and ectoenzyme release of the LLC-PK1 cells from pig, effective for the investigation of the function of the glycosyl-phosphatidylinositol-anchor protein
molecular biology
-
enzyme is used as a tool in the studies of GPI-anchored proteins
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taguchi, R.; Asahi, Y.; Ikezawa, H.
Purification and properties of phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis
Biochim. Biophys. Acta
619
48-57
1980
Bacillus thuringiensis
Koke, J.A.; Yang, M.; Henner, D.J.; Volwerk, J.J.; Griffith, O.H.
High-level expression in Escherichia coli and rapid purification of phosphatidylinositol-specific phospholipase C from Bacillus cereus and Bacillus thuringiensis
Protein Expr. Purif.
2
51-58
1991
Bacillus cereus, Bacillus thuringiensis
Itami, C.; Kimura, Y.; Taguchi, R.; Ikezawa, H.; Nakayashi, T.
Growth inhibition, morphological change, and ectoenzyme release of LLC-PK1 cells by phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis
Biosci. Biotechnol. Biochem.
61
776-781
1997
Bacillus thuringiensis
Wehbi, H.; Feng, J.; Kolbeck, J.; Ananthanarayanan, B.; Cho, W.; Roberts, M.F.
Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C
Biochemistry
42
9374-9382
2003
Bacillus thuringiensis
Wehbi, H.; Feng, J.; Roberts, M.F.
Water-miscible organic cosolvents enhance phosphatidylinositol-specific phospholipase C phosphotransferase as well as phosphodiesterase activity
Biochim. Biophys. Acta
1613
15-27
2003
Bacillus thuringiensis
Feng, J.; Wehbi, H.; Roberts, M.F.
Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C
J. Biol. Chem.
277
19867-19875
2002
Bacillus thuringiensis
Feng, J.; Bradley, W.D.; Roberts, M.F.
Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C
J. Biol. Chem.
278
24651-24657
2003
Bacillus thuringiensis
Zhao, L.; Liao, H; Tsai, M.D.
The catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad in phosphatidylinositol-specific phospholipase C can be substituted by a chloride-ion
J. Biol. Chem.
279
31995-32000
2004
Bacillus thuringiensis
Ikezawa, H.
Bacterial phosphatidylinositol-specific phospholipase C as membrane-attacking agents and tools for research on GPI-anchored proteins
J. Toxicol. Toxin Rev.
23
479-508
2004
Bacillus cereus, Bacillus thuringiensis, Listeria monocytogenes, Staphylococcus aureus
-
Guo, S.; Zhang, X.; Seaton, B.A.; Roberts, M.F.
Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C
Biochemistry
47
4201-4210
2008
Bacillus thuringiensis (P08954)
Pu, M.; Roberts, M.F.; Gershenson, A.
Fluorescence correlation spectroscopy of phosphatidylinositol-specific phospholipase C monitors the interplay of substrate and activator lipid binding
Biochemistry
48
6835-6845
2009
Bacillus thuringiensis
Shi, X.; Shao, C.; Zhang, X.; Zambonelli, C.; Redfield, A.G.; Head, J.F.; Seaton, B.A.; Roberts, M.F.
Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface
J. Biol. Chem.
284
15607-15618
2009
Bacillus thuringiensis (P08954)
Cheng, J.; Karri, S.; Grauffel, C.; Wang, F.; Reuter, N.; Roberts, M.F.; Wintrode, P.L.; Gershenson, A.
Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding?
Biophys. J.
104
185-195
2013
Bacillus thuringiensis (P08954), Bacillus thuringiensis N168C (P08954)
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