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Information on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase
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EC Tree
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 enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
phosphatidylinositol-specific plc, pi-phospholipase c, 1-phosphatidylinositol phosphodiesterase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming)
-
-
-
-
1-phosphatidylinositol phosphodiesterase
-
-
-
-
EC 3.1.4.10
-
-
formerly
-
monophosphatidylinositol phosphodiesterase
-
-
-
-
Phosphatidylinositol diacylglycerol-lyase
-
-
-
-
phosphatidylinositol phosphodiesterase
-
-
-
-
phosphatidylinositol phospholipase C
-
-
-
-
phosphatidylinositol-specific phospholipase C
PI-PLC
PLC1
PLC2
PLC3
PLC4
phosphatidylinositol-specific phospholipase C
-
-
-
-
phosphatidylinositol-specific phospholipase C
-
phosphatidylinositol-specific phospholipase C
-
-
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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
-
-
-
-
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
mechanism
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37288-19-0
-
63551-76-8
-
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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
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
-
-
?
dihexanoylphosphorothioyl-myo-inositol
myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate + 1,2-dihexanoyl-sn-glycerol
-
-
-
-
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
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
-
-
?
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
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natural aggregate substrate, PI-PLC is a virulence factor of the animal and human pathogen
-
?
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
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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
?
-
-
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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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
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
-
natural substrate
-
?
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
-
?
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
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
activates R69D mutant at low concentrations, no activation of wild-type PI-PLC
Co2+
-
activates R69D mutant at low concentrations, no activation of wild-type PI-PLC
Li+
-
5fold activation of R69D mutant, slight activation of wild-type PI-PLC
Mg2+
Mn2+
-
activates R69D mutant at low concentrations, slight activation of wild-type PI-PLC
Sr2+
-
9fold activation of R69D mutant, slight activation of wild-type PI-PLC
additional information
Ca2+
-
41fold activation of R69D mutant, slight activation of wild-type PI-PLC
Mg2+
-
35fold activation of R69D mutant, slight activation of wild-type PI-PLC
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ET-18-OCH3
-
specific inhibitors of PI-PLC, 0.1 mM abolish stimulatory effect of 0.00005 mM heme in the PI-PLC/protein kinase C pathway
U73122
-
specific inhibitors of PI-PLC, 0.05 mM abolish stimulatory effect of heme in the PI-PLC/protein kinase C pathway
Zn2+
-
severe inhibition of wild-type PI-PLC, complete inhibition of R69D mutant below 1 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
diacylglycerol
-
activates, increases the hydrolytic activity of PI-PLC on large unilamellar vesicles containing 5-40% phosphatidylinositol
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Glioma
Potentiation of stimulus-induced phosphoinositide breakdown by calmodulin antagonists in C6 glioma cells.
Infections
Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection.
Neoplasms
Macrophages target Listeria monocytogenes by two discrete non-canonical autophagy pathways.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
methyl-fluorescein myo-inositol phosphate
-
pH 7, 25°C, in presence of dihexanoylphosphatidylcholine
0.81
methyl-fluorescein myo-inositol phosphate
-
pH 7, 25°C, in absence of dihexanoylphosphatidylcholine
additional information
additional information
-
kinetics of butyl-fluorescein myo-inositol phosphate and methyl-fluorescein myo-inositol phosphate cleavage, two-site kinetic model
-
additional information
additional information
-
kinetics, two-site kinetic model
-
additional information
additional information
phospholipid binding kinetics of the recombinant enzyme, ooverview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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)
2.9
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
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
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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
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phosphotransferase activity towards phosphatidylinositol in several aggregation states in the absence and presence of 30% isopropanol
additional information
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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