Information on EC 4.6.1.13 - phosphatidylinositol diacylglycerol-lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
4.6.1.13
-
RECOMMENDED NAME
GeneOntology No.
phosphatidylinositol diacylglycerol-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
show the reaction diagram
-
-
-
-
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
show the reaction diagram
mechanism
-
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
show the reaction diagram
general acid/general base mechanism
-
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
show the reaction diagram
mechanism
-
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
P-O bond cleavage
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Inositol phosphate metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
P08954
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific phospholipase C
-
-
phosphatidylinositol-specific PLC
-
-
phosphatidylinositolphospholipase C
-
-
PI-phospholipase C
-
-
PI-PLC
P34024
-
PI-PLC
P34024
-
-
PI-PLC
Paramecium tetraurelia d4-2
-
-
-
PLC1
Paramecium tetraurelia d4-2
-
-
-
PLC2
Paramecium tetraurelia d4-2
-
-
-
PLC3
Paramecium tetraurelia d4-2
-
-
-
PLC4
Paramecium tetraurelia d4-2
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37288-19-0
-
63551-76-8
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
with PLC2 and PLC6, RNAi phenotypes show strong defects in release of GPI-anchored surface proteins in vivo
malfunction
Paramecium tetraurelia d4-2
-
with PLC2 and PLC6, RNAi phenotypes show strong defects in release of GPI-anchored surface proteins in vivo
-
physiological function
-
for highly anionic membranes, but not phosphatidylcholine-rich vesicles, binding correlates well with relative activity
physiological function
-
PI-PLC pathway is involved in the stimulatory effect of heme on (Na+ + K+)ATPase via PKC-like activation
physiological function
-
acute incubation of Cos-7 cells for 1 h with PI-PLC significantly reduces the amount of cell-surface expression, both of 5'-nucleotidase by 31.9% and of expressed alpha2delta-2 by 49.4%. PI-PLC treatment reduces calcium current density when alpha2delta subunits are coexpressed. PI-PLC treatment of hippocampal lysates reduces the detergent-resistant membrane association of alpha2delta-1 from 68.3% to 8.3%, and also resultes in recovery of alpha2-1 in the aqueous phase after Triton X-114 separation. Incubation of cultured dorsal root-ganglion neurons for 60 min with PI-PLC substantially reduces cell surface alpha2delta-1 immunofluorescence. It does not reduce that for the transmembrane p75 nerve growth-factor receptor
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
-
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
natural substrate
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the active site is located at the C-terminal side
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
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
show the reaction diagram
-
natural aggregate substrate, PI-PLC is a virulence factor of the animal and human pathogen
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + sn-1,2-diacylglycerol
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
dihexanoylphosphorothioyl-myo-inositol
myo-inositol cis(2-OH,S)-1,6-cyclic phosphorothioate + 1,2-dihexanoyl-sn-glycerol
show the reaction diagram
-
-
-
-
?
lysophosphatidylinositol + H2O
?
show the reaction diagram
-
-
-
-
?
lysophosphatidylinositol + H2O
?
show the reaction diagram
-
-
-
-
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
show the reaction diagram
-
monomeric substrate, only the D-enantiomer is active
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
-
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
myo-inositol-1,2-cyclic phosphate appears as sole product
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
specific for
-
?
phosphatidylinositol + H2O
diacylglycerol + myo-inositol 1,2-cyclic phosphate
show the reaction diagram
-
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
show the reaction diagram
-
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 + D-myo-inositol 1-phosphate
show the reaction diagram
-
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
-
-
?
methyl-fluorescein myo-inositol phosphate
D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein
show the reaction diagram
-
substrate binds only to the active site and not to the activator site
-
?
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
-
additional information
?
-
-
the enzyme may have a role in Bacillus anthracis pathogenesis, enzyme from Bacillus anthracis unlike the ortholog from Listeria monocytogenes shows high activity on glycosylphosphatidylinositol-anchored proteins
-
-
-
additional information
?
-
P34024
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
?
-
-
Lys44 mediates the initial electrostatic interaction of the protein with substrate
-
-
-
additional information
?
-
-
Phe237 is a key residue in the very tight binding of PI-PLC to membranes containing anionic phospholipids
-
-
-
additional information
?
-
-
PI-PLC does not affect control transmembrane or membrane-associated proteins
-
-
-
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
?
-
P34024
ability to facilitate escape from the macrophage phagosome, is dependent on host PKCbeta
-
-
-
additional information
?
-
Paramecium tetraurelia d4-2
-
all PLCs are able to cleave GPI anchors
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
natural substrate
-
?
1-phosphatidyl-1D-myo-inositol
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
show the reaction diagram
-
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
?
-
-
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
?
-
-
the enzyme exhibits cytotoxicity against some cultivated cells
-
-
-
additional information
?
-
-
the enzyme may have a role in Bacillus anthracis pathogenesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
41fold activation of R69D mutant, slight activation of wild-type PI-PLC
Cd2+
-
activates R69D mutant at low concentrations, no activation of wild-type PI-PLC
Cl-
-
1 M, 2-3fold 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+
-
35fold activation of R69D mutant, slight activation of wild-type PI-PLC
Mg2+
-
MgCl2, activates
Sr2+
-
9fold activation of R69D mutant, slight activation of wild-type PI-PLC
Mn2+
-
activates R69D mutant at low concentrations, slight activation of wild-type PI-PLC
additional information
-
no requirement for a divalent metal ion
additional information
-
wild-type PI-PLC is calcium-independent
additional information
-
Ca2+-independent
additional information
-
salts have an activity-enhancing effect
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AOT
-
bis(2-ethylhexyl)sulfosuccinate
-
Ca2+
-
2-5 mM, 50% inhibition
Cd2+
-
severe inhibition of wild-type PI-PLC
Co2+
-
severe inhibition of wild-type PI-PLC
ET-18-OCH(3)
-
specific inhibitors of PI-PLC, 0.1 mM abolish stimulatory effect of 0.00005 mM heme in the PI-PLC/protein kinase C pathway
Mg2+
-
2-5 mM, 50% inhibition
Mn2+
-
2-5 mM, 50% inhibition
myo-Inositol
-
weak
myo-Inositol
-
poor competitive inhibitor
NaCl
-
at high concentrations
Ni2+
-
severe inhibition of wild-type PI-PLC
p-chloromercuriphenylsulfonic-acid
-
-
U73122
-
specific inhibitors of PI-PLC, 0.05 mM abolish stimulatory effect of heme in the PI-PLC/protein kinase C pathway
Zn2+
-
2-5 mM, 50% inhibition
Zn2+
-
severe inhibition of wild-type PI-PLC, complete inhibition of R69D mutant below 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
deoxycholate
-
stimulates
diacylglycerol
-
activates
diacylglycerol
-
activates, increases the hydrolytic activity of PI-PLC on large unilamellar vesicles containing 5-40% phosphatidylinositol
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
Isopropanol
-
water-miscible, maximum activation at 30%, activates regardless of the type of phosphatidylinositol substrate, enhances phosphotransferase activity
Isopropanol
-
30%, activates
Isopropanol
-
water-miscible, 30%, activates
phosphatidic acid
-
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidycholine
-
-
-
phosphatidylcholine
-
binding to nonsubstrate zwitterionic phosphatidylcholine interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
phosphatidylcholine
-
activates
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
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
SDS
-
strongly activates
Triton X-100
-
stimulates
Triton X-100
-
stimulates
Tween 20
-
slight stimulation
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
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.061
-
methyl-fluorescein myo-inositol phosphate
-
pH 7
0.14
-
methyl-fluorescein myo-inositol phosphate
-
pH 7, 25C, in presence of dihexanoylphosphatidylcholine
1.4
-
phosphatidylinositol
-
-
0.81
-
methyl-fluorescein myo-inositol phosphate
-
pH 7, 25C, in absence of dihexanoylphosphatidylcholine
additional information
-
additional information
-
kinetics, two-site kinetic model
-
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
-
kinetic data
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
66
-
methyl-fluorescein myo-inositol phosphate
-
pH 7
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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)
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
6.7
-
-
mutant Y247S/Y251S, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
9.5
-
-
wild-type, with phosphatidylinositol as substrate, in the presence of 2 mM POPC (for the small unilamellar vesicles)
13.74
-
-
-
30
-
-
pH 7.2, phosphatidylinositol as substrate, in absence of MgCl2
41
-
-
mutant Y247S/Y251S, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
62
-
-
mutant Y246S/Y247S/Y248S/Y251S, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
73
-
-
wild-type, with 8 mM cIP as substrate, in the presence of 5 mM diheptanoylphosphatidylcholine
98
-
-
mutant Y246S/Y247S/Y248S, with phosphatidylinositol as substrate, in the presence of 16 mM Triton X-100
112
-
-
mutant Y246S/Y247S/Y248S/Y251S, with phosphatidylinositol as substrate, in the presence of 32 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
401
-
-
W47I mutant PI-PLC, phosphotransferase activity
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
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
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 28C
3560
-
-
pH 7.5, 37C, wild-type PI-PLC, in absence of Ca2+
additional information
-
-
-
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
-
-
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
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
wild-type PI-PLC, in the absence of 1 M Cl-
7
7.2
-
assay at
7
8
-
wild-type PI-PLC, in the presence of 1 M Cl-
7
-
-
assay at
7.1
-
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
7.2
7.5
-
-
7.5
-
-
assay at
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
39
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
70
-
20C: about 80% of maximal activity, 70C: about 35% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-
theoretical pI
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant PI-PLC, expressed in Escherichia coli BL21
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
Staphylococcus aureus (strain Newman)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23000
-
-
gel filtration
23000
-
-
nondenaturing PAGE
28200
-
-
laser light scattering
29000
-
-
gel filtration
33000
-
-
sequence analysis
34460
-
-
R69C mutant PI-PLC, electrospray ionization mass spectrometry
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 15000, alpha-peptide, + x * 23000, beta-peptide, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 35000
monomer
-
although small amounts of dimer have been noted previously
monomer
-
1 * 28000, in solution, laser light scattering
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with myo-inositol
-
X-ray crystal structure
-
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
-
wild-type and D274N mutant PI-PLC
-
recombinant PI-PLC
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
some thermal unfolding of PI-PLC occurs
30
-
-
Tm-value in presence of 30% isopropanol, myo-inositol enhances thermostability in isopropanol
41.5
-
-
Tm-value, pH 8, W178A mutant PI-PLC
47
-
-
Tm-value, pH 8, W280A mutant PI-PLC
50
-
-
pH 8.0, 30 min, stable below
53.6
-
-
Tm-value in absence of 30% isopropanol
53.6
-
-
Tm-value, pH 8, W47A mutant PI-PLC
54.4
-
-
Tm-value, pH 8, wild-type PI-PLC
54.4
-
-
Tm-value, wild-type PI-PLC
54.6
-
-
Tm-value, pH 8, W47A/W242A double mutant PI-PLC
56.2
-
-
Tm-value, pH 8, W242A mutant PI-PLC
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
myo-inositol stabilizes
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
isopropanol
-
water/isopropanol mixture decreases stability, at 4C 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 30C, myo-inositol enhances thermostability in isopropanol
isopropanol
-
water-miscible, 30%, activates
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type and mutant PI-PLC
-
PI-PLC mutants
-
R69C mutant PI-PLC
-
Q-sepharose fast-flow column and phenyl-Sepharose column, monitored by SDS-PAGE
-
recombinant PI-PLC
-
recombinant wild-type and mutant PI-PLC
-
wild-type and mutant PI-PLC
-
wild-type and mutants, by gel filtration
-
by sonication and centrifugation, on chitin column and by gel filtration, more than 85% pure
-
recombinant PI-PLC
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Listeria monocytogenes. Listeria monocytogenes expressing Bacillus anthracis phosphatidylinositol-specific phospholipase C shows significantly decreased efficiencies of ascape from a phagosome and in cell-to-cell spread
-
expression in Escherichia coli, construction of four vectors for high-level expression
-
expression in Escherichia coli MM294
-
expression in Escherichia coli, construction of four vectors for high-level expression
-
overexpressed in Escherichia coli
-
overexpression in Escherichia coli BL21
-
transformed into Escherichia coli BL21-Codonplus (DE3)-RIL cells
-
wild-type and mutant PI-PLC, expression in Escherichia coli BL21
-
wild-type and mutants overexpressed in Escherichia coli
-
inserted into the pTYB11 N-terminal fusion vector between Sap I and EcoR I restriction sites. Recombinant plasmid, IMPACT-Y, transformed into Escherichia coli ER2566 cells for overexpression
-
PI-PLC gene is part of the virulence gene cluster, overexpression in Escherichia coli MM294
-
cloned into the L4440 vector, transformation of plasmids into Escherichia coli HT115DE3
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PLC5 reveals a drastic lower mRNA level compared to all other PLCs, this gene shows characteristics of a non-functional pseudogene. Adequate knockdown levels for almost all PLCs in the RNAi lines, except for PLC5 with only 53.85%
-
PLC2, PLC4 and PLC6 show the highest mRNA levels
-
PLC5 reveals a drastic lower mRNA level compared to all other PLCs, this gene shows characteristics of a non-functional pseudogene. Adequate knockdown levels for almost all PLCs in the RNAi lines, except for PLC5 with only 53.85%
Paramecium tetraurelia d4-2
-
-
PLC2, PLC4 and PLC6 show the highest mRNA levels
Paramecium tetraurelia d4-2
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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+
R69A
-
mutant is specifically activated by guanidinium hydrochloride
R69A
-
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
R69C
-
mutation of the catalytic Arg-69, not activated by 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+
R69G
-
mutant is specifically activated by guanidinium hydrochloride
R69G
-
mutation of the catalytic Arg-69, 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
G48A
-
single mutant
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
I43A
-
single mutant
I43W
-
single mutant
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
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
L39A
-
single mutant
L39A/V46A
-
are made by introducing the second mutation in the gene coding for a single mutant
N168C
-
1% relative activity
N243W/W242A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
P42G
-
single mutant
P42G
-
0.7% relative activity; impaired phosphatidylcholine binding, but still binds most tightly to mixed lipid vesicles
Q45A
-
single mutant
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
V46A
-
single mutant
W178A
-
mutant with reduced stability and specific activity, study of kinetic activation by micellar phosphatidylcholine
W242A
-
interfacial binding study
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
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
-
interfacial binding study
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, 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
W47F
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
W47I
-
kinetic analysis, binding studies to phosphatidylcholine vesicles
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
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
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
DP-L1552
P34024
genotype, deltaplcA. Phenotype PI-PLC-
DP-L1935
P34024
genotype, deltaplcb. Phenotype PC-PLC-
DP-L1936
P34024
genotype, deltaplcA/deltaplcB. Phenotype PI-PLC-/PC-PLC-
DP-L2161
P34024
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)
-
M49W/W47A
-
double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
-
enzyme is used as a tool in the studies of GPI-anchored proteins
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
medicine
-
PI-PLC is a virulence factor of the animal and human pathogen causing listeriosis
molecular biology
-
enzyme is used as a tool in the studies of GPI-anchored proteins
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