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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 + diacylglycerol
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + sn-1,2-diacylglycerol
-
natural aggregate substrate, two-site enzyme model with interfacial cooperativity between the active site and a lipid-binding subsite, presumably adjacent to the active site
-
?
butyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + butyl-fluorescein
-
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
-
?
dibutyrylphosphatidylinositol
1D-myo-inositol 1,2-(cyclic)-phosphate + 1,2-dibutyryl-sn-glycerol
-
is a poor substrate, necessitating long incubation times (2 to 5 h) if the same enzyme concentration is to be used in the absence and presence of salts and amphiphiles
-
-
?
dihexanoylphosphatidyl inositol
?
-
-
-
-
?
dihexanoylphosphorothioyl-myo-inositol
myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate + 1,2-dihexanoyl-sn-glycerol
-
-
-
-
?
lysophosphatidylinositol + H2O
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate + D-myo-inositol 1-phosphate
-
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
?
-
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
-
-
-
?
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 + diacylglycerol
-
-
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
natural substrate
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
a catalytic diad at the active site composed of Asp-274 and His-32 is involved in substrate-assisted catalysis, its function is to hydrogen-bond with the 2-OH of phosphatidylinositol to form a catalytic triad, catalytic mechanism
PI-PLC catalyzes in a second step the slow hydrolysis of 1D-myo-inositol 1,2-cyclic phosphate to form myo-inositol 1-phosphate
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
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
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
catalytic mechanism, role of Arg-69, the bidentate nature of Arg-69 is the origin of the large thio effects and stereoselectivity in PI-PLC, its function is to bring the phosphate group and the 2-OH group of inositol into proximity and to induce proper alignment for nucleophilic attack, and possibly to lower the pKa of the 2-OH
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
PLC accepts only nonphosphorylated phosphatidylinositol substrates and produces cyclic inositol phosphate as final product, which is hydrolyzed at a 1000fold lower rate, catalytic mechanism, uses a guanidinium group of Arg-69 during catalysis
-
?
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
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
-
natural aggregate substrate, PI-PLC is a virulence factor of the animal and human pathogen
-
?
lysophosphatidylinositol + H2O
?
-
-
-
-
?
lysophosphatidylinositol + H2O
?
-
-
-
-
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
-
substrate binds only to the active site and not to the activator site
-
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
-
monomeric substrate, only the D-enantiomer is active
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
diacylglycerol and a mixture of myo-inositol 1-phosphate and myo-inositol 1,2-cyclic 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
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
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
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
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
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
-
specific for
-
?
additional information
?
-
-
Bacillus anthracis enzyme down-modulates dendritic cell function und T cell responses, possibly by cleaving GPI-anchored proteins important for TLR-mediated dendritic cell activation
-
-
?
additional information
?
-
-
the enzyme may have a role in Bacillus anthracis pathogenesis
-
-
?
additional information
?
-
-
enzyme from Bacillus anthracis unlike the ortholog from Listeria monocytogenes shows high activity on glycosylphosphatidylinositol-anchored proteins
-
-
?
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
?
-
-
not: phosphatidylcholine
-
?
additional information
?
-
-
not: phosphatidylcholine
-
?
additional information
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
?
additional information
?
-
-
Lys44 mediates the initial electrostatic interaction of the protein with substrate
-
-
?
additional information
?
-
-
Listeria monocytogenes phosphatidylinositol-specific phospholipase C is an important determinant of Listeria monocytogenes pathogenesis by absence of the Vb beta-strand, thus leading to greatly reduced activity on GPI-anchored proteins
-
-
?
additional information
?
-
-
the enzyme activates a host protein kinase C cascade which promotes escape of the bacterium from a macrophage-like cell phagosome
-
-
?
additional information
?
-
-
the enzyme contributes to listerial infection of epithelial cells and macrophages as a virulence factor cooperating with other factors such as listeriolysin O and phosphatidylcholine-preferring phospholipase C
-
-
?
additional information
?
-
ability to facilitate escape from the macrophage phagosome, is dependent on host PKCbeta
-
-
?
additional information
?
-
-
Phe237 is a key residue in the very tight binding of PI-PLC to membranes containing anionic phospholipids
-
-
?
additional information
?
-
ability to facilitate escape from the macrophage phagosome, is dependent on host PKCbeta
-
-
?
additional information
?
-
-
all PLCs are able to cleave GPI anchors
-
-
?
additional information
?
-
-
all PLCs are able to cleave GPI anchors
-
-
?
additional information
?
-
formation of inositol 1,2-(cyclic)phosphate from L-alpha-phoshatidylinositol, NMR spectroscopy analysis
-
-
?
additional information
?
-
-
synthesis of short-chain (dihexanoyl) analogues of phosphatidylinositol as substrates. The intermediate is generated from dihexanoylphosphorothioyl-myo-inositol identified as myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate. The cyclic intermediate is gradually hydrolyzed to inositol 1-phosphorothioate. Both the Rp and Sp isomers of the phosphorodithioate analogue are readily cleaved, with the Sp isomer being hydrolyzed only ca. 6times more slowly than the Rp isomer. Rates of cleavage of two other substrates in which the pro-S oxygen is left unaltered, dihexanoylphosphorothioyl-myo-inositol and dihexanoylphosphatidyl inositol, are affected to only a small extent (0.6 and 1.6-fold, respectively) by the analogous modification of the bridging position. Strong Sp thio effect arises from a loss of a catalytic interaction rather than a steric effect
-
-
?
additional information
?
-
-
PI-PLC does not affect control transmembrane or membrane-associated proteins
-
-
?
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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
diethyl ether
-
strongly activates
diheptanoyl phosphatidylcholine
-
activates
dihexanoyl phosphatidylcholine
-
activates, 4-5fold increase in catalytic efficiency, binds to a lipid-binding subsite, not to the active site, maximal activation at 0.4 mM
dihexanoylphosphatidylcholine
-
non-substrate activator lipid, maximum PI-PLC activity at 0.7-1 mM
dimethylformamide
-
water-miscible, enhances phosphotransferase activity
Dimethylsulfoxide
-
water-miscible, enhances phosphotransferase activity
ethanol
-
all PLC1-6 are activated in salt/ethanol extractions
heme
-
heme receptor mediates the stimulatory effect of heme on the (Na+ + K+)ATPase activity through a PIPLC/PKC signaling pathway
KCl
-
ionic strength, and not the salt identity, is important for PI-PLC activation towards phosphatidylinositol in micelles. Added salt has a synergistic effect with zwitterionic phospholipids, leading to high specific activities for phosphatidylinositol cleavage with only moderate dilution of the anionic substrate in the interface. This kinetic activation correlates with weakening of strong PI-PLC hydrophobic interactions with the interface. PI-PLC cleavage of phosphatidylinositol presented in small unilamellar vesicles is activated by salt
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
Salt
-
all PLC1-6 are activated in salt/ethanol extractions
Tween 20
-
slight stimulation
deoxycholate
-
stimulates
diacylglycerol
-
activates, increases the hydrolytic activity of PI-PLC on large unilamellar vesicles containing 5-40% phosphatidylinositol
diacylglycerol
-
activates
Isopropanol
-
30%, activates
Isopropanol
-
water-miscible, 30%, activates
Isopropanol
-
water-miscible, maximum activation at 30%, activates regardless of the type of phosphatidylinositol substrate, enhances phosphotransferase activity
phosphatidylcholine
-
phosphatidylcholine
-
activates
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
Triton X-100
-
stimulates
Triton X-100
-
stimulates
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
-
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0.2
mutant Y246S/Y247S/Y248S, with 8 mM cIP as substrate
0.4
mutant Y246S/Y247S/Y248S/Y251S, with 8 mM cIP as substrate
0.6
mutant Y247S/Y251S, with 8 mM cIP as substrate
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
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
2.1
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
2.3
wild-type, with 8 mM cIP as substrate
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
30
-
pH 7.2, phosphatidylinositol as substrate, in absence of MgCl2
301
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
3560
-
pH 7.5, 37°C, wild-type PI-PLC, in absence of Ca2+
375
wild-type, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
401
-
W47I mutant PI-PLC, phosphotransferase activity
41
mutant Y247S/Y251S, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
556
-
wild-type PI-PLC, phosphotransferase activity
558
-
W47F mutant PI-PLC, phosphotransferase activity
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
658
-
W242F mutant PI-PLC, phosphotransferase activity
670
mutant Y247S/Y251S, with phosphatidylinositol as substrate, in the presence of 32 mM diheptanoylphosphatidylcholine
684
-
W242I mutant PI-PLC, phosphotransferase activity
700 - 1300
-
pH 7.2, phosphatidylinositol as substrate, in presence of MgCl2
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
additional information
-
-
additional information
-
-
additional information
-
values for wild-type and several mutant PI-PLCs in presence of 0.1 mM or 1 mM Ca2+ and in absence of Ca2+
additional information
-
-
additional information
-
-
additional information
-
-
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
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D274A
-
mutation of an catalytic diad residue, mutant with abolished activity, NMR study
D274N
-
mutation of an catalytic diad residue, 4.2% of wild-type activity
H32A
-
mutation of an catalytic diad residue, mutant with abolished activity, NMR study
D33N/R69D
-
PI-PLC double mutant, 50fold activation by 1 mM Ca2+
R69D
-
reduced activity compared with wild-type enzyme, mutant is activated by Ca2+, mutation engineers a catalytic metal binding site into the calcium-independent PI-PLC leading to enhanced stereoselectivity
R69E
-
mutation of the catalytic Arg-69, inactive mutant, not activated by Ca2+
R69N
-
mutation of the catalytic Arg-69, not activated by Ca2+
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
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
M49W/W47A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
N168C
-
1% relative activity
N243W/W242A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
P245Y
the mutant shows reduced activity and membrane affinity
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
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
W47F
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
W47I
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
Y246A
the variant shows significant membrane binding defects
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/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
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
Y247A
the variant shows significant membrane binding defects
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
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
P245Y
-
the mutant shows reduced activity and membrane affinity
-
Y246A
-
the variant shows significant membrane binding defects
-
Y246A/Y247A
-
the variant shows significant membrane binding defects
-
Y247A
-
the variant shows significant membrane binding defects
-
Y86A/Y88A
-
the mutations decrease membrane affinity for the enzyme
-
DP-L1552
genotype, deltaplcA. Phenotype PI-PLC-
DP-L1935
genotype, deltaplcb. Phenotype PC-PLC-
DP-L1936
genotype, deltaplcA/deltaplcB. Phenotype PI-PLC-/PC-PLC-
DP-L2161
genotype, deltahyl. Phenotype LLO- (listeriolysin O)
F237A
-
most approaches wild-type PI-PLC in its dependence on enzyme concentration
F237W
-
even at high concentrations, has high specific activity comparable to dilute unaltered recombinant PI-PLC, does not form the aggregates with anionic lipid-rich vesicles that are disrupted by excess detergent and salt, although it is still activated to about the same extent as wild-type by salt
L151A
-
added KCl (0.15 M) still enhances PI-PLC cleavage of phosphatidylinositol in TX-100 micelles, although KCl effects are much more modest (1.6fold increase) compared to wild-type, F237A or F237W
L235A
-
added KCl (0.15 M) still enhances PI-PLC cleavage of phosphatidylinositol in TX-100 micelles, although KCl effects are much more modest (1.4fold increase) compared to wild-type, F237A or F237W
W49A
-
added KCl (0.15 M) still enhances PI-PLC cleavage of phosphatidylinositol in TX-100 micelles, although KCl effects are much more modest (1.8fold increase) compared to wild-type, F237A or F237W
DP-L1552
-
genotype, deltaplcA. Phenotype PI-PLC-
-
DP-L1935
-
genotype, deltaplcb. Phenotype PC-PLC-
-
DP-L1936
-
genotype, deltaplcA/deltaplcB. Phenotype PI-PLC-/PC-PLC-
-
DP-L2161
-
genotype, deltahyl. Phenotype LLO- (listeriolysin O)
-
F249W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
H86E
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
H86Y
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
V44C
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
V44W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253K
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253S
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y253S/Y255S
site-directed mutagenesis, the mutant has the same secondary structure content but a 5°C lower thermal denaturation temperature than the wild-type and an altered enzyme activity
Y253W
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
Y290A
site-directed mutagenesis, the mutant shows no significant changes in structure and thermal stability, but altered enzyme activity compared to the wild-type enzyme
R69A
-
mutant is specifically activated by guanidinium hydrochloride
R69A
-
mutation of the catalytic Arg-69, not activated by Ca2+
R69C
-
mutation of the catalytic Arg-69, not activated by Ca2+
R69C
-
site-directed chemical modification of the cysteine residue replacing Arg-69, mutant PI-PLCs featuring bidentate side chains at this position display significantly higher activity, higher thio effects, and greater stereoselectivity than do those with monodentate side chains
R69G
-
mutant is specifically activated by guanidinium hydrochloride
R69G
-
mutation of the catalytic Arg-69, not activated by Ca2+
K44A
-
interfacial binding study
K44A
-
0.98% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles
K44E
single mutant
K44E
-
0.44% relative activity. Has dramatically diminished affinity for phosphatidylglycerol-rich vesicles and slightly reduced affinity for phosphatidylcholine-rich vesicles
P42G
single mutant
P42G
-
0.7% relative activity
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
-
interfacial binding study
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
-
interfacial binding study
W47A
-
mutant with much weaker binding to interfaces and lower kinetic interfacial activation
W47A/W242A
-
double mutant, interfacial binding study
W47A/W242A
-
double mutant, no affinity for phospholipid surfaces, no kinetic activation by micellar phosphatidylcholine
W47A/W242A
dimeric mutant, which is unable to bind to phosphatidycholine
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
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
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